A species of gram-negative, aerobic bacteria first isolated from soil in Vineland, New Jersey. Ammonium and nitrate are used as nitrogen sources by this bacterium. It is distinguished from other members of its genus by the ability to use rhamnose as a carbon source. (From Bergey's Manual of Determinative Bacteriology, 9th ed)
A genus of gram-negative, aerobic bacteria found in soil and water. Its organisms occur singly, in pairs or irregular clumps, and sometimes in chains of varying lengths.
An enzyme system that catalyzes the fixing of nitrogen in soil bacteria and blue-green algae (CYANOBACTERIA). EC 1.18.6.1.
A non-heme iron-sulfur protein isolated from Clostridium pasteurianum and other bacteria. It is a component of NITROGENASE, which is active in nitrogen fixation, and consists of two subunits with molecular weights of 59.5 kDa and 50.7 kDa, respectively.
The process in certain BACTERIA; FUNGI; and CYANOBACTERIA converting free atmospheric NITROGEN to biologically usable forms of nitrogen, such as AMMONIA; NITRATES; and amino compounds.
Iron-containing proteins that transfer electrons, usually at a low potential, to flavoproteins; the iron is not present as in heme. (McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
A low-molecular-weight (16,000) iron-free flavoprotein containing one molecule of flavin mononucleotide (FMN) and isolated from bacteria grown on an iron-deficient medium. It can replace ferredoxin in all the electron-transfer functions in which the latter is known to serve in bacterial cells.
A metallic element with the atomic symbol Mo, atomic number 42, and atomic weight 95.94. It is an essential trace element, being a component of the enzymes xanthine oxidase, aldehyde oxidase, and nitrate reductase. (From Dorland, 27th ed)
Acetylene is not typically considered a medical term, but rather a chemical compound (C2H2) commonly used in industrial and laboratory settings for its high energy content and reactivity, which may have various applications in medicine such as wound healing and surgical procedures, but it is not a medical diagnosis or disease.
A non-heme iron-sulfur protein isolated from Clostridium pasteurianum and other bacteria. It is a component of NITROGENASE along with molybdoferredoxin and is active in nitrogen fixation.
Salts of alginic acid that are extracted from marine kelp and used to make dental impressions and as absorbent material for surgical dressings.
The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)
Enzymes that catalyze the epimerization of chiral centers within carbohydrates or their derivatives. EC 5.1.3.
A metallic element with the atomic symbol V, atomic number 23, and atomic weight 50.94. It is used in the manufacture of vanadium steel. Prolonged exposure can lead to chronic intoxication caused by absorption usually via the lungs.
Salts and esters of hydroxybutyric acid.
The functional hereditary units of BACTERIA.
A multienzyme complex responsible for the formation of ACETYL COENZYME A from pyruvate. The enzyme components are PYRUVATE DEHYDROGENASE (LIPOAMIDE); dihydrolipoamide acetyltransferase; and LIPOAMIDE DEHYDROGENASE. Pyruvate dehydrogenase complex is subject to three types of control: inhibited by acetyl-CoA and NADH; influenced by the energy state of the cell; and inhibited when a specific serine residue in the pyruvate decarboxylase is phosphorylated by ATP. PYRUVATE DEHYDROGENASE (LIPOAMIDE)-PHOSPHATASE catalyzes reactivation of the complex. (From Concise Encyclopedia Biochemistry and Molecular Biology, 3rd ed)
Proteins found in any species of bacterium.
Cytochromes (electron-transporting proteins) with a tetrapyrrolic chelate of iron as a prosthetic group in which the degree of conjugation of double bonds is less than in porphyrin. (From Enzyme Nomenclature, 1992, p539)
Tungsten. A metallic element with the atomic symbol W, atomic number 74, and atomic weight 183.85. It is used in many manufacturing applications, including increasing the hardness, toughness, and tensile strength of steel; manufacture of filaments for incandescent light bulbs; and in contact points for automotive and electrical apparatus.
An enzyme that catalyzes the transfer of the planetary sulfur atom of thiosulfate ion to cyanide ion to form thiocyanate ion. EC 2.8.1.1.
A flavoprotein containing oxidoreductase that catalyzes the reduction of lipoamide by NADH to yield dihydrolipoamide and NAD+. The enzyme is a component of several MULTIENZYME COMPLEXES.
Term used to designate tetrahydroxy aldehydic acids obtained by oxidation of hexose sugars, i.e. glucuronic acid, galacturonic acid, etc. Historically, the name hexuronic acid was originally given to ascorbic acid.
A complex of enzymes and PROTON PUMPS located on the inner membrane of the MITOCHONDRIA and in bacterial membranes. The protein complex provides energy in the form of an electrochemical gradient, which may be used by either MITOCHONDRIAL PROTON-TRANSLOCATING ATPASES or BACTERIAL PROTON-TRANSLOCATING ATPASES.
Reversibly catalyze the oxidation of a hydroxyl group of carbohydrates to form a keto sugar, aldehyde or lactone. Any acceptor except molecular oxygen is permitted. Includes EC 1.1.1.; EC 1.1.2.; and 1.1.99.
A technique applicable to the wide variety of substances which exhibit paramagnetism because of the magnetic moments of unpaired electrons. The spectra are useful for detection and identification, for determination of electron structure, for study of interactions between molecules, and for measurement of nuclear spins and moments. (From McGraw-Hill Encyclopedia of Science and Technology, 7th edition) Electron nuclear double resonance (ENDOR) spectroscopy is a variant of the technique which can give enhanced resolution. Electron spin resonance analysis can now be used in vivo, including imaging applications such as MAGNETIC RESONANCE IMAGING.
Resorcinols are aromatic organic compounds containing two hydroxyl groups attached to a benzene ring, known for their antiseptic and antibacterial properties, used in various medical and cosmetic applications.
An enzyme that catalyzes the acetyltransferase reaction using ACETYL CoA as an acetyl donor and dihydrolipoamide as acceptor to produce COENZYME A (CoA) and S-acetyldihydrolipoamide. It forms the (E2) subunit of the PYRUVATE DEHYDROGENASE COMPLEX.
Proteins that have one or more tightly bound metal ions forming part of their structure. (Dorland, 28th ed)
A sugar acid formed by the oxidation of the C-6 carbon of GLUCOSE. In addition to being a key intermediate metabolite of the uronic acid pathway, glucuronic acid also plays a role in the detoxification of certain drugs and toxins by conjugating with them to form GLUCURONIDES.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
A group of proteins possessing only the iron-sulfur complex as the prosthetic group. These proteins participate in all major pathways of electron transport: photosynthesis, respiration, hydroxylation and bacterial hydrogen and nitrogen fixation.
A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Flavoproteins are a type of protein molecule that contain noncovalently bound flavin mononucleotide or flavin adenine dinucleotide as cofactors, involved in various redox reactions and metabolic pathways, such as electron transfer, energy production, and DNA repair.
The first chemical element in the periodic table. It has the atomic symbol H, atomic number 1, and atomic weight [1.00784; 1.00811]. It exists, under normal conditions, as a colorless, odorless, tasteless, diatomic gas. Hydrogen ions are PROTONS. Besides the common H1 isotope, hydrogen exists as the stable isotope DEUTERIUM and the unstable, radioactive isotope TRITIUM.
An enzyme found in bacteria. It catalyzes the reduction of FERREDOXIN and other substances in the presence of molecular hydrogen and is involved in the electron transport of bacterial photosynthesis.
A metallic element with atomic symbol Fe, atomic number 26, and atomic weight 55.85. It is an essential constituent of HEMOGLOBINS; CYTOCHROMES; and IRON-BINDING PROTEINS. It plays a role in cellular redox reactions and in the transport of OXYGEN.
Hemeproteins whose characteristic mode of action involves transfer of reducing equivalents which are associated with a reversible change in oxidation state of the prosthetic group. Formally, this redox change involves a single-electron, reversible equilibrium between the Fe(II) and Fe(III) states of the central iron atom (From Enzyme Nomenclature, 1992, p539). The various cytochrome subclasses are organized by the type of HEME and by the wavelength range of their reduced alpha-absorption bands.
An element with the atomic symbol N, atomic number 7, and atomic weight [14.00643; 14.00728]. Nitrogen exists as a diatomic gas and makes up about 78% of the earth's atmosphere by volume. It is a constituent of proteins and nucleic acids and found in all living cells.
The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.
The rate dynamics in chemical or physical systems.
The Ketoglutarate Dehydrogenase Complex is a multi-enzyme complex involved in the citric acid cycle, catalyzing the oxidative decarboxylation of alpha-ketoglutarate to succinyl-CoA and CO2, thereby connecting the catabolism of amino acids, carbohydrates, and fats to the generation of energy in the form of ATP.
Gram-negative, non-motile, capsulated, gas-producing rods found widely in nature and associated with urinary and respiratory infections in humans.
Dithionite. The dithionous acid ion and its salts.
Organic compounds that are acyclic and contain three acid groups. A member of this class is citric acid which is the first product formed by reaction of pyruvate and oxaloacetate. (From Lehninger, Principles of Biochemistry, 1982, p443)
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
1,1'-Bis(phenylmethyl)4,4'-bipyridinium dichloride. Oxidation-reduction indicator.
Any of the processes by which cytoplasmic or intercellular factors influence the differential control of gene action in bacteria.
Used in the form of the hydrochloride as a reagent in ANALYTICAL CHEMISTRY TECHNIQUES.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
A dye used as a reagent in the determination of vitamin C.
Thulium. An element of the rare earth family of metals. It has the atomic symbol Tm, atomic number 69, and atomic weight 168.93.
Deoxyribonucleic acid that makes up the genetic material of bacteria.
The process by which ELECTRONS are transported from a reduced substrate to molecular OXYGEN. (From Bennington, Saunders Dictionary and Encyclopedia of Laboratory Medicine and Technology, 1984, p270)
A family of compounds containing an oxo group with the general structure of 1,5-pentanedioic acid. (From Lehninger, Principles of Biochemistry, 1982, p442)
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Proteins, usually acting in oxidation-reduction reactions, containing iron but no porphyrin groups. (Lehninger, Principles of Biochemistry, 1993, pG-10)
Inorganic salts of the hypothetical acid, H3Fe(CN)6.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
A genus of motile or nonmotile gram-positive bacteria of the family Clostridiaceae. Many species have been identified with some being pathogenic. They occur in water, soil, and in the intestinal tract of humans and lower animals.
Derivatives of ammonium compounds, NH4+ Y-, in which all four of the hydrogens bonded to nitrogen have been replaced with hydrocarbyl groups. These are distinguished from IMINES which are RN=CR2.
A condensation product of riboflavin and adenosine diphosphate. The coenzyme of various aerobic dehydrogenases, e.g., D-amino acid oxidase and L-amino acid oxidase. (Lehninger, Principles of Biochemistry, 1982, p972)
Any liquid or solid preparation made specifically for the growth, storage, or transport of microorganisms or other types of cells. The variety of media that exist allow for the culturing of specific microorganisms and cell types, such as differential media, selective media, test media, and defined media. Solid media consist of liquid media that have been solidified with an agent such as AGAR or GELATIN.
Enzymes catalyzing the transfer of an acetyl group, usually from acetyl coenzyme A, to another compound. EC 2.3.1.
Solution titration in which the end point is read from the electrode-potential variations with the concentrations of potential determining ions. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Used as an electron carrier in place of the flavine enzyme of Warburg in the hexosemonophosphate system and also in the preparation of SUCCINIC DEHYDROGENASE.
An element that is a member of the chalcogen family. It has an atomic symbol S, atomic number 16, and atomic weight [32.059; 32.076]. It is found in the amino acids cysteine and methionine.
An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.
An enzyme that catalyzes the oxidation and reduction of FERREDOXIN or ADRENODOXIN in the presence of NADP. EC 1.18.1.2 was formerly listed as EC 1.6.7.1 and EC 1.6.99.4.
Inorganic salts of HYDROGEN CYANIDE containing the -CN radical. The concept also includes isocyanides. It is distinguished from NITRILES, which denotes organic compounds containing the -CN radical.
Polymers of organic acids and alcohols, with ester linkages--usually polyethylene terephthalate; can be cured into hard plastic, films or tapes, or fibers which can be woven into fabrics, meshes or velours.
The protein components of a number of complexes, such as enzymes (APOENZYMES), ferritin (APOFERRITINS), or lipoproteins (APOLIPOPROTEINS).
A highly poisonous compound that is an inhibitor of many metabolic processes, but has been shown to be an especially potent inhibitor of heme enzymes and hemeproteins. It is used in many industrial processes.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
The measurement of the amplitude of the components of a complex waveform throughout the frequency range of the waveform. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
Spectroscopic method of measuring the magnetic moment of elementary particles such as atomic nuclei, protons or electrons. It is employed in clinical applications such as NMR Tomography (MAGNETIC RESONANCE IMAGING).
Vibrio- to spiral-shaped phototrophic bacteria found in stagnant water and mud exposed to light.
An element with atomic symbol O, atomic number 8, and atomic weight [15.99903; 15.99977]. It is the most abundant element on earth and essential for respiration.
A family of signal transducing adaptor proteins that control the METABOLISM of NITROGEN. They are primarily found in prokaryotes.
Adenosine 5'-(trihydrogen diphosphate). An adenine nucleotide containing two phosphate groups esterified to the sugar moiety at the 5'-position.
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Determination of the spectra of ultraviolet absorption by specific molecules in gases or liquids, for example Cl2, SO2, NO2, CS2, ozone, mercury vapor, and various unsaturated compounds. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
A colorless alkaline gas. It is formed in the body during decomposition of organic materials during a large number of metabolically important reactions. Note that the aqueous form of ammonia is referred to as AMMONIUM HYDROXIDE.
An enzyme that catalyzes the oxidation of nitrite to nitrate. It is a cytochrome protein that contains IRON and MOLYBDENUM.
Derivatives of ACETIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxymethane structure.
An enzyme that catalyzes the conversion of ATP, L-glutamate, and NH3 to ADP, orthophosphate, and L-glutamine. It also acts more slowly on 4-methylene-L-glutamate. (From Enzyme Nomenclature, 1992) EC 6.3.1.2.
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
A spectroscopic technique which uses the Mossbauer effect (inelastic scattering of gamma radiation resulting from interaction with heavy nuclei) to monitor the small variations in the interaction between an atomic nucleus and its environment. Such variations may be induced by changes in temperature, pressure, chemical state, molecular conformation, molecular interaction, or physical site. It is particularly useful for studies of structure-activity relationship in metalloproteins, mobility of heavy metals, and the state of whole tissue and cell membranes.
Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.
Enzymes that catalyze the cleavage of a carbon-sulfur bond by means other than hydrolysis or oxidation. EC 4.4.
'Methylamines' are organic compounds consisting of a methyl group (CH3) linked to an amino group (-NH2), with the general formula of CH3-NH-R, where R can be a hydrogen atom or any organic group, and they exist as colorless gases or liquids at room temperature.
Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.
A genus of gram-negative, ovoid to rod-shaped bacteria that is phototrophic. All species use ammonia as a nitrogen source. Some strains are found only in sulfide-containing freshwater habitats exposed to light while others may occur in marine, estuarine, and freshwater environments.
Use of restriction endonucleases to analyze and generate a physical map of genomes, genes, or other segments of DNA.
A basic science concerned with the composition, structure, and properties of matter; and the reactions that occur between substances and the associated energy exchange.
The rate at which oxygen is used by a tissue; microliters of oxygen STPD used per milligram of tissue per hour; the rate at which oxygen enters the blood from alveolar gas, equal in the steady state to the consumption of oxygen by tissue metabolism throughout the body. (Stedman, 25th ed, p346)
In bacteria, a group of metabolically related genes, with a common promoter, whose transcription into a single polycistronic MESSENGER RNA is under the control of an OPERATOR REGION.
The sum of the weight of all the atoms in a molecule.
Enzymes which transfer sulfur atoms to various acceptor molecules. EC 2.8.1.
The composition, conformation, and properties of atoms and molecules, and their reaction and interaction processes.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
A coenzyme for a number of oxidative enzymes including NADH DEHYDROGENASE. It is the principal form in which RIBOFLAVIN is found in cells and tissues.
The heritable modification of the properties of a competent bacterium by naked DNA from another source. The uptake of naked DNA is a naturally occuring phenomenon in some bacteria. It is often used as a GENE TRANSFER TECHNIQUE.

Pseudomonas aeruginosa killing of Caenorhabditis elegans used to identify P. aeruginosa virulence factors. (1/366)

We reported recently that the human opportunistic pathogen Pseudomonas aeruginosa strain PA14 kills Caenorhabditis elegans and that many P. aeruginosa virulence factors (genes) required for maximum virulence in mouse pathogenicity are also required for maximum killing of C. elegans. Here we report that among eight P. aeruginosa PA14 TnphoA mutants isolated that exhibited reduced killing of C. elegans, at least five also exhibited reduced virulence in mice. Three of the TnphoA mutants corresponded to the known virulence-related genes lasR, gacA, and lemA. Three of the mutants corresponded to known genes (aefA from Escherichia coli, pstP from Azotobacter vinelandii, and mtrR from Neisseria gonorrhoeae) that had not been shown previously to play a role in pathogenesis, and two of the mutants contained TnphoA inserted into novel sequences. These data indicate that the killing of C. elegans by P. aeruginosa can be exploited to identify novel P. aeruginosa virulence factors important for mammalian pathogenesis.  (+info)

The recombinant Azotobacter vinelandii mannuronan C-5-epimerase AlgE4 epimerizes alginate by a nonrandom attack mechanism. (2/366)

The Ca2+-dependent mannuronan C-5-epimerase AlgE4 is a representative of a family of Azotobacter vinelandii enzymes catalyzing the polymer level epimerization of beta-D-mannuronic acid (M) to alpha-L-guluronic acid (G) in the commercially important polysaccharide alginate. The reaction product of recombinantly produced AlgE4 is predominantly characterized by an alternating sequence distribution of the M and G residues (MG blocks). AlgE4 was purified after intracellular overexpression in Escherichia coli, and the activity was shown to be optimal at pH values between 6.5 and 7.0, in the presence of 1-3 mM Ca2+, and at temperatures near 37 degrees C. Sr2+ was found to substitute reasonably well for Ca2+ in activation, whereas Zn2+ strongly inhibited the activity. During epimerization of alginate, the fraction of GMG blocks increased linearly as a function of the total fraction of G residues and comparably much faster than that of MMG blocks. These experimental data could not be accounted for by a random attack mechanism, suggesting that the enzyme either slides along the alginate chain during catalysis or recognizes a pre-existing G residue as a preferred substrate in its consecutive attacks.  (+info)

Requirement of NifX and other nif proteins for in vitro biosynthesis of the iron-molybdenum cofactor of nitrogenase. (3/366)

The iron-molybdenum cofactor (FeMo-co) of nitrogenase contains molybdenum, iron, sulfur, and homocitrate in a ratio of 1:7:9:1. In vitro synthesis of FeMo-co has been established, and the reaction requires an ATP-regenerating system, dithionite, molybdate, homocitrate, and at least NifB-co (the metabolic product of NifB), NifNE, and dinitrogenase reductase (NifH). The typical in vitro FeMo-co synthesis reaction involves mixing extracts from two different mutant strains of Azotobacter vinelandii defective in the biosynthesis of cofactor or an extract of a mutant strain complemented with the purified missing component. Surprisingly, the in vitro synthesis of FeMo-co with only purified components failed to generate significant FeMo-co, suggesting the requirement for one or more other components. Complementation of these assays with extracts of various mutant strains demonstrated that NifX has a role in synthesis of FeMo-co. In vitro synthesis of FeMo-co with purified components is stimulated approximately threefold by purified NifX. Complementation of these assays with extracts of A. vinelandii DJ42. 48 (DeltanifENX DeltavnfE) results in a 12- to 15-fold stimulation of in vitro FeMo-co synthesis activity. These data also demonstrate that apart from the NifX some other component(s) is required for the cofactor synthesis. The in vitro synthesis of FeMo-co with purified components has allowed the detection, purification, and identification of an additional component(s) required for the synthesis of cofactor.  (+info)

The A modules of the Azotobacter vinelandii mannuronan-C-5-epimerase AlgE1 are sufficient for both epimerization and binding of Ca2+. (4/366)

The industrially important polysaccharide alginate is composed of the two sugar monomers beta-D-mannuronic acid (M) and its epimer alpha-L-guluronic acid (G). In the bacterium Azotobacter vinelandii, the G residues originate from a polymer-level reaction catalyzed by one periplasmic and at least five secreted mannuronan C-5-epimerases. The secreted enzymes are composed of repeats of two protein modules designated A (385 amino acids) and R (153 amino acids). The modular structure of one of the epimerases, AlgE1, is A1R1R2R3A2R4. This enzyme has two catalytic sites for epimerization, each site introducing a different G distribution pattern, and in this article we report the DNA-level construction of a variety of truncated forms of the enzyme. Analyses of the properties of the corresponding proteins showed that an A module alone is sufficient for epimerization and that A1 catalyzed the formation of contiguous stretches of G residues in the polymer, while A2 introduces single G residues. These differences are predicted to strongly affect the physical and immunological properties of the reaction product. The epimerization reaction is Ca2+ dependent, and direct binding studies showed that both the A and R modules bind this cation. The R modules appeared to reduce the Ca2+ concentration needed for full activity and also stimulated the reaction rate when positioned both N and C terminally.  (+info)

Incorporation of molybdenum into the iron-molybdenum cofactor of nitrogenase. (5/366)

The biosynthesis of the iron-molybdenum cofactor (FeMo-co) of dinitrogenase was investigated using 99Mo to follow the incorporation of Mo into precursors. 99Mo label accumulates on dinitrogenase only when all known components of the FeMo-co synthesis system, NifH, NifNE, NifB-cofactor, homocitrate, MgATP, and reductant, are present. Furthermore, 99Mo label accumulates only on the gamma protein, which has been shown to serve as a chaperone/insertase for the maturation of apodinitrogenase when all known components are present. It appears that only completed FeMo-co can accumulate on the gamma protein. Very little FeMo-co synthesis was observed when all known components are used in purified forms, indicating that additional factors are required for optimal FeMo-co synthesis. 99Mo did not accumulate on NifNE under any conditions tested, suggesting that Mo enters the pathway at some other step, although it remains possible that a Mo-containing precursor of FeMo-co that is not sufficiently stable to persist during gel electrophoresis occurs but is not observed. 99Mo accumulates on several unidentified species, which may be the additional components required for FeMo-co synthesis. The molybdenum storage protein was observed and the accumulation of 99Mo on this protein required nucleotide.  (+info)

Evidence that MgATP accelerates primary electron transfer in a Clostridium pasteurianum Fe protein-Azotobacter vinelandii MoFe protein nitrogenase tight complex. (6/366)

The nitrogenase catalytic cycle involves binding of the iron (Fe) protein to the molybdenum-iron (MoFe) protein, transfer of a single electron from the Fe protein to the MoFe protein concomitant with the hydrolysis of at least two MgATP molecules, followed by dissociation of the two proteins. Earlier studies found that combining the Fe protein isolated from the bacterium Clostridium pasteurianum with the MoFe protein isolated from the bacterium Azotobacter vinelandii resulted in an inactive, nondissociating Fe protein-MoFe protein complex. In the present work, it is demonstrated that primary electron transfer occurs within this nitrogenase tight complex in the absence of MgATP (apparent first-order rate constant k = 0.007 s-1) and that MgATP accelerates this electron transfer reaction by more than 10,000-fold to rates comparable to those observed within homologous nitrogenase complexes (k = 100 s-1). Electron transfer reactions were confirmed by EPR spectroscopy. Finally, the midpoint potentials (Em) for the Fe protein [4Fe-4S]2+/+ cluster and the MoFe protein P2+/N cluster were determined for both the uncomplexed and complexed proteins and with or without MgADP. Calculations from electron transfer theory indicate that the measured changes in Em are not likely to be sufficient to account for the observed nucleotide-dependent rate accelerations for electron transfer.  (+info)

A vanadium and iron cluster accumulates on VnfX during iron-vanadium-cofactor synthesis for the vanadium nitrogenase in Azotobacter vinelandii. (7/366)

The vnf-encoded nitrogenase from Azotobacter vinelandii contains an iron-vanadium cofactor (FeV-co) in its active site. Little is known about the synthesis pathway of FeV-co, other than that some of the gene products required are also involved in the synthesis of the iron-molybdenum cofactor (FeMo-co) of the widely studied molybdenum-dinitrogenase. We have found that VnfX, the gene product of one of the genes contained in the vnf-regulon, accumulates iron and vanadium in a novel V-Fe cluster during synthesis of FeV-co. The electron paramagnetic resonance (EPR) and metal analyses of the V-Fe cluster accumulated on VnfX are consistent with a VFe7-8Sx precursor of FeV-co. The EPR spectrum of VnfX with the V-Fe cluster bound strongly resembles that of isolated FeV-co and a model VFe3S4 compound. The V-Fe cluster accumulating on VnfX does not contain homocitrate. No accumulation of V-Fe cluster on VnfX was observed in strains with deletions in genes known to be involved in the early steps of FeV-co synthesis, suggesting that it corresponds to a precursor of FeV-co. VnfX purified from a nifB strain incapable of FeV-co synthesis has a different electrophoretic mobility in native anoxic gels than does VnfX, which has the V-Fe cluster bound. NifB-co, the Fe and S precursor of FeMo-co (and presumably FeV-co), binds to VnfX purified from the nifB strain, producing a shift in its electrophoretic mobility on anoxic native gels. The data suggest that a precursor of FeV-co that contains vanadium and iron accumulates on VnfX, and thus, VnfX is involved in the synthesis of FeV-co.  (+info)

In vitro biosynthesis of iron-molybdenum cofactor and maturation of the nif-encoded apodinitrogenase. Effect of substitution for NifH with site-specifically altered forms of NifH. (8/366)

NifH has three different roles in the nitrogenase enzyme system. Apart from serving as the physiological electron donor to dinitrogenase, NifH is involved in iron-molybdenum cofactor (FeMo-co) biosynthesis and in maturation of the FeMo-co-deficient form of apodinitrogenase to a FeMo-co-activable form (apodinitrogenase maturation). The exact roles of NifH in these processes are not well understood. In the present study, the features of NifH required for the aforementioned processes have been investigated by the use of site-specifically altered forms of the enzyme. The ability of six altered forms of NifH inactive in substrate reduction (K15R, D39N, D43N, L127Delta, D129E, and F135Y) to function in in vitro FeMo-co synthesis and apodinitrogenase maturation reactions was investigated. We report that the ability of NifH to bind and not hydrolyze MgATP is required for it to function in these processes. We also present evidence that the ability of NifH to function in these processes is not dictated by the properties known to be required for its function in electron transfer to dinitrogenase. Evidence toward the existence of separate, overlapping sites on NifH for each of its functions (substrate reduction, FeMo-co biosynthesis, and apodinitrogenase maturation) is presented.  (+info)

'Azotobacter vinelandii' is a species of free-living, nitrogen-fixing bacteria that is commonly found in soil and freshwater environments. The name 'Azotobacter' comes from the Greek words "azoto," meaning "nitrogen," and "bakterion," meaning "rod" or "staff," while "vinelandii" refers to Vineland, New Jersey, where the bacterium was first isolated.

'Azotobacter vinelandii' is known for its ability to convert atmospheric nitrogen gas (N2) into ammonia (NH3), a process called nitrogen fixation. This makes it an important contributor to the global nitrogen cycle and a valuable tool in agricultural and industrial applications.

In addition to its nitrogen-fixing abilities, 'Azotobacter vinelandii' is also known for its resistance to desiccation, high tolerance to oxygen levels, and ability to produce various extracellular polysaccharides and enzymes. These characteristics make it a popular model organism for studying bacterial metabolism, stress responses, and genetic regulation.

Overall, 'Azotobacter vinelandii' is a fascinating and important microorganism with significant implications for our understanding of the nitrogen cycle, environmental biology, and potential industrial applications.

'Azotobacter' is a genus of free-living nitrogen-fixing bacteria commonly found in soil and water. These bacteria are capable of converting atmospheric nitrogen into ammonia, a process known as nitrogen fixation, which can then be used by plants for growth. The name 'Azotobacter' comes from the Greek words "azoto," meaning without life, and "bakterion," meaning little rod.

The bacteria are characterized by their ability to form cysts or thick-walled resting stages that allow them to survive in unfavorable conditions such as dryness or high temperatures. They are also known for their large size, typically ranging from 1.5 to 2.5 micrometers in diameter, and their motility, which is powered by a single polar flagellum.

'Azotobacter' species are important contributors to the nitrogen cycle in soil and play a crucial role in maintaining soil fertility. They have also been studied for their potential use in various industrial applications, such as the production of biofuels, bioplastics, and enzymes.

Nitrogenase is not a medical term, but a biological term used in the field of microbiology and biochemistry. It refers to an enzyme complex found in certain bacteria and archaea that have the ability to fix nitrogen gas (N2) from the atmosphere into ammonia (NH3), a form of nitrogen that can be utilized by plants and other organisms for growth and development. This process is known as biological nitrogen fixation, which is essential for maintaining the global nitrogen cycle and supporting life on Earth.

The medical field may refer to nitrogenase in relation to human health in the context of understanding the role of nitrogen-fixing bacteria in soil fertility and their impact on agriculture and food production. However, there is no direct medical definition or application for nitrogenase.

Molybdoferredoxin is not a widely recognized medical term, but it is a term used in biochemistry and molecular biology to describe a type of protein that contains molybdenum and iron-sulfur clusters as cofactors. These proteins are involved in various redox reactions in the body, particularly in the metabolism of certain amino acids, nucleotides, and other small molecules.

Molybdoferredoxins are found in many organisms, including bacteria, archaea, and eukaryotes (including humans). In humans, molybdoferredoxins play important roles in several metabolic pathways, such as the oxidation of sulfite to sulfate and the reduction of nitrate to nitrite.

Deficiencies or mutations in molybdoferredoxin-related genes can lead to various metabolic disorders, including molybdenum cofactor deficiency, a rare genetic disorder that affects multiple enzymes requiring molybdenum as a cofactor.

Nitrogen fixation is a process by which nitrogen gas (N2) in the air is converted into ammonia (NH3) or other chemically reactive forms, making it available to plants and other organisms for use as a nutrient. This process is essential for the nitrogen cycle and for the growth of many types of plants, as most plants cannot utilize nitrogen gas directly from the air.

In the medical field, nitrogen fixation is not a commonly used term. However, in the context of microbiology and infectious diseases, some bacteria are capable of fixing nitrogen and this ability can contribute to their pathogenicity. For example, certain species of bacteria that colonize the human body, such as those found in the gut or on the skin, may be able to fix nitrogen and use it for their own growth and survival. In some cases, these bacteria may also release fixed nitrogen into the environment, which can have implications for the ecology and health of the host and surrounding ecosystems.

Ferredoxins are iron-sulfur proteins that play a crucial role in electron transfer reactions in various biological systems, particularly in photosynthesis and nitrogen fixation. They contain one or more clusters of iron and sulfur atoms (known as the iron-sulfur cluster) that facilitate the movement of electrons between different molecules during metabolic processes.

Ferredoxins have a relatively simple structure, consisting of a polypeptide chain that binds to the iron-sulfur cluster. This simple structure allows ferredoxins to participate in a wide range of redox reactions and makes them versatile electron carriers in biological systems. They can accept electrons from various donors and transfer them to different acceptors, depending on the needs of the cell.

In photosynthesis, ferredoxins play a critical role in the light-dependent reactions by accepting electrons from photosystem I and transferring them to NADP+, forming NADPH. This reduced form of nicotinamide adenine dinucleotide phosphate (NADPH) is then used in the Calvin cycle for carbon fixation and the production of glucose.

In nitrogen fixation, ferredoxins help transfer electrons to the nitrogenase enzyme complex, which reduces atmospheric nitrogen gas (N2) into ammonia (NH3), making it available for assimilation by plants and other organisms.

Overall, ferredoxins are essential components of many metabolic pathways, facilitating electron transfer and energy conversion in various biological systems.

Flavodoxin is not strictly a medical term, but it is a term used in biochemistry and molecular biology. Flavodoxins are small electron transfer proteins that contain a non-heme iron atom bound to a organic molecule called flavin mononucleotide (FMN). They play a role in various biological processes such as photosynthesis, nitrogen fixation and respiration where they function as electron carriers. Flavodoxins can undergo reversible oxidation and reduction, and this property allows them to transfer electrons between different enzymes during metabolic reactions. They are not specific to human physiology, but can be found in various organisms including bacteria, algae, and plants.

I'm sorry for any confusion, but "Molybdenum" is not a medical term. It is an element with the symbol Mo and atomic number 42 on the periodic table. Molybdenum is used in various industries, including medicine, for example in the production of surgical instruments and some prosthetics due to its strength and resistance to corrosion. However, it is not a term used to describe a medical condition or bodily process. If you have any questions related to elements and their uses in medicine, I'd be happy to help with those!

Acetylene is defined as a colorless, highly flammable gas with a distinctive odor, having the chemical formula C2H2. It is the simplest and lightest hydrocarbon in which two carbon atoms are bonded together by a triple bond. Acetylene is used as a fuel in welding and cutting torches, and it can also be converted into other chemicals, such as vinyl acetate and acetic acid. In medical terms, acetylene is not a substance that is commonly used or discussed.

Dinitrogenase reductase is a protein involved in the process of nitrogen fixation in certain bacteria and archaea. It is responsible for delivering electrons to the enzyme dinitrogenase, which converts atmospheric nitrogen (N2) into ammonia (NH3), making it available for use by living organisms. Dinitrogenase reductase contains a cluster of iron and sulfur atoms that facilitate the transfer of electrons. The combined action of dinitrogenase reductase and dinitrogenase allows these microorganisms to utilize nitrogen from the atmosphere as a source of nitrogen for growth, making them important contributors to the global nitrogen cycle.

Alginates are a type of polysaccharide derived from brown algae or produced synthetically, which have gelling and thickening properties. In medical context, they are commonly used as a component in wound dressings, dental impressions, and bowel cleansing products. The gels formed by alginates can provide a protective barrier to wounds, help maintain a moist environment, and promote healing. They can also be used to create a mold of the mouth or other body parts in dental and medical applications. In bowel cleansing, sodium alginates are often combined with sodium bicarbonate and water to form a solution that expands and stimulates bowel movements, helping to prepare the colon for procedures such as colonoscopy.

Oxidoreductases are a class of enzymes that catalyze oxidation-reduction reactions, which involve the transfer of electrons from one molecule (the reductant) to another (the oxidant). These enzymes play a crucial role in various biological processes, including energy production, metabolism, and detoxification.

The oxidoreductase-catalyzed reaction typically involves the donation of electrons from a reducing agent (donor) to an oxidizing agent (acceptor), often through the transfer of hydrogen atoms or hydride ions. The enzyme itself does not undergo any permanent chemical change during this process, but rather acts as a catalyst to lower the activation energy required for the reaction to occur.

Oxidoreductases are classified and named based on the type of electron donor or acceptor involved in the reaction. For example, oxidoreductases that act on the CH-OH group of donors are called dehydrogenases, while those that act on the aldehyde or ketone groups are called oxidases. Other examples include reductases, peroxidases, and catalases.

Understanding the function and regulation of oxidoreductases is important for understanding various physiological processes and developing therapeutic strategies for diseases associated with impaired redox homeostasis, such as cancer, neurodegenerative disorders, and cardiovascular disease.

Carbohydrate epimerases are a group of enzymes that catalyze the interconversion of specific stereoisomers (epimers) of carbohydrates by the reversible oxidation and reduction of carbon atoms, usually at the fourth or fifth position. These enzymes play important roles in the biosynthesis and modification of various carbohydrate-containing molecules, such as glycoproteins, proteoglycans, and glycolipids, which are involved in numerous biological processes including cell recognition, signaling, and adhesion.

The reaction catalyzed by carbohydrate epimerases involves the transfer of a hydrogen atom and a proton between two adjacent carbon atoms, leading to the formation of new stereochemical configurations at these positions. This process can result in the conversion of one epimer into another, thereby expanding the structural diversity of carbohydrates and their derivatives.

Carbohydrate epimerases are classified based on the type of substrate they act upon and the specific stereochemical changes they induce. Some examples include UDP-glucose 4-epimerase, which interconverts UDP-glucose and UDP-galactose; UDP-N-acetylglucosamine 2-epimerase, which converts UDP-N-acetylglucosamine to UDP-N-acetylmannosamine; and GDP-fucose synthase, which catalyzes the conversion of GDP-mannose to GDP-fucose.

Understanding the function and regulation of carbohydrate epimerases is crucial for elucidating their roles in various biological processes and developing strategies for targeting them in therapeutic interventions.

I'm sorry for any confusion, but "Vanadium" is not a medical term. It is a chemical element with the symbol V and atomic number 23. Vanadium is not a biological or medical concept in itself, but it can be found in some living organisms in small amounts as a trace element.

However, vanadium compounds have been studied in the context of potential medicinal uses, such as insulin mimetic properties and possible effects on diabetes management. But these are still in the research stage and not yet established medical facts or practices. Therefore, I would be happy to provide more information about vanadium from a chemical or materials science perspective, but it is not typically considered within the realm of medical definitions.

Hydroxybutyrates are compounds that contain a hydroxyl group (-OH) and a butyric acid group. More specifically, in the context of clinical medicine and biochemistry, β-hydroxybutyrate (BHB) is often referred to as a "ketone body."

Ketone bodies are produced by the liver during periods of low carbohydrate availability, such as during fasting, starvation, or a high-fat, low-carbohydrate diet. BHB is one of three major ketone bodies, along with acetoacetate and acetone. These molecules serve as alternative energy sources for the brain and other tissues when glucose levels are low.

In some pathological states, such as diabetic ketoacidosis, the body produces excessive amounts of ketone bodies, leading to a life-threatening metabolic acidosis. Elevated levels of BHB can also be found in other conditions like alcoholism, severe illnesses, and high-fat diets.

It is important to note that while BHB is a hydroxybutyrate, not all hydroxybutyrates are ketone bodies. The term "hydroxybutyrates" can refer to any compound containing both a hydroxyl group (-OH) and a butyric acid group.

A bacterial gene is a segment of DNA (or RNA in some viruses) that contains the genetic information necessary for the synthesis of a functional bacterial protein or RNA molecule. These genes are responsible for encoding various characteristics and functions of bacteria such as metabolism, reproduction, and resistance to antibiotics. They can be transmitted between bacteria through horizontal gene transfer mechanisms like conjugation, transformation, and transduction. Bacterial genes are often organized into operons, which are clusters of genes that are transcribed together as a single mRNA molecule.

It's important to note that the term "bacterial gene" is used to describe genetic elements found in bacteria, but not all genetic elements in bacteria are considered genes. For example, some DNA sequences may not encode functional products and are therefore not considered genes. Additionally, some bacterial genes may be plasmid-borne or phage-borne, rather than being located on the bacterial chromosome.

The Pyruvate Dehydrogenase Complex (PDC) is a multi-enzyme complex that plays a crucial role in cellular energy metabolism. It is located in the mitochondrial matrix and catalyzes the oxidative decarboxylation of pyruvate, the end product of glycolysis, into acetyl-CoA. This reaction links the carbohydrate metabolism (glycolysis) to the citric acid cycle (Krebs cycle), enabling the continuation of energy production in the form of ATP through oxidative phosphorylation.

The Pyruvate Dehydrogenase Complex consists of three main enzymes: pyruvate dehydrogenase (E1), dihydrolipoyl transacetylase (E2), and dihydrolipoyl dehydrogenase (E3). Additionally, two regulatory enzymes are associated with the complex: pyruvate dehydrogenase kinase (PDK) and pyruvate dehydrogenase phosphatase (PDP). These regulatory enzymes control the activity of the PDC through reversible phosphorylation and dephosphorylation, allowing the cell to adapt to varying energy demands and substrate availability.

Deficiencies or dysfunctions in the Pyruvate Dehydrogenase Complex can lead to various metabolic disorders, such as pyruvate dehydrogenase deficiency, which may result in neurological impairments and lactic acidosis due to disrupted energy metabolism.

Bacterial proteins are a type of protein that are produced by bacteria as part of their structural or functional components. These proteins can be involved in various cellular processes, such as metabolism, DNA replication, transcription, and translation. They can also play a role in bacterial pathogenesis, helping the bacteria to evade the host's immune system, acquire nutrients, and multiply within the host.

Bacterial proteins can be classified into different categories based on their function, such as:

1. Enzymes: Proteins that catalyze chemical reactions in the bacterial cell.
2. Structural proteins: Proteins that provide structural support and maintain the shape of the bacterial cell.
3. Signaling proteins: Proteins that help bacteria to communicate with each other and coordinate their behavior.
4. Transport proteins: Proteins that facilitate the movement of molecules across the bacterial cell membrane.
5. Toxins: Proteins that are produced by pathogenic bacteria to damage host cells and promote infection.
6. Surface proteins: Proteins that are located on the surface of the bacterial cell and interact with the environment or host cells.

Understanding the structure and function of bacterial proteins is important for developing new antibiotics, vaccines, and other therapeutic strategies to combat bacterial infections.

Cytochromes d are a group of electron transport proteins that contain heme as a cofactor and are involved in redox reactions. They are classified as part of the cytochrome system, which is a series of electron carriers that transfer electrons from one molecule to another during cellular respiration and other metabolic processes.

The cytochromes d group includes several different proteins, such as cytochrome d, cytochrome d1, and cytochrome d2. These proteins are found in various organisms, including bacteria, archaea, and mitochondria of eukaryotic cells. They typically have a relatively low redox potential and play a role in the terminal electron acceptor step of anaerobic respiration, where they transfer electrons to oxygen or other electron acceptors.

It's worth noting that cytochromes d are less well-studied compared to other cytochrome groups such as cytochromes a, b, and c. Therefore, the medical relevance of this group may be limited, but they still play important roles in various biological processes.

I'm sorry for any confusion, but 'Tungsten' is not a medical term. It is a chemical element with the symbol W and atomic number 74. Tungsten is a rare metal found naturally on Earth, and it has many industrial uses due to its hardness, high density, and high melting point.

In the context of medicine or healthcare, tungsten may be encountered in certain medical devices, such as X-ray tubes and electrodes, where its properties are utilized for their durability and heat resistance. However, it is not a term that would typically have a formal medical definition.

Thiosulfate Sulfurtransferase (TST) is an enzyme that catalyzes the transfer of a sulfur group from thiosulfate to a range of acceptor molecules. It plays a crucial role in the detoxification of harmful substances and the maintenance of cellular redox balance. TST is also known as Rhodanese, which comes from the Greek word "rhodanos," meaning rose-red, due to the pinkish-red color of the enzyme when it was first isolated.

The systematic medical definition of Thiosulfate Sulfurtransferase is:

A mitochondrial matrix enzyme (EC 2.8.1.1) that catalyzes the transfer of a sulfur atom from thiosulfate to cyanide, forming thiocyanate and sulfite. This reaction serves as a detoxification pathway for cyanide in the body. TST also plays a role in maintaining cellular redox balance by participating in the reduction of oxidized proteins and other molecules.

Dihydrolipoamide dehydrogenase (DHLD) is an enzyme that plays a crucial role in several important metabolic pathways in the human body, including the citric acid cycle and the catabolism of certain amino acids. DHLD is a component of multi-enzyme complexes, such as the pyruvate dehydrogenase complex (PDC) and the alpha-ketoglutarate dehydrogenase complex (KGDC).

The primary function of DHLD is to catalyze the oxidation of dihydrolipoamide, a reduced form of lipoamide, back to its oxidized state (lipoamide) while simultaneously reducing NAD+ to NADH. This reaction is essential for the continued functioning of the PDC and KGDC, as dihydrolipoamide is a cofactor for these enzyme complexes.

Deficiencies in DHLD can lead to serious metabolic disorders, such as maple syrup urine disease (MSUD) and riboflavin-responsive multiple acyl-CoA dehydrogenase deficiency (RR-MADD). These conditions can result in neurological symptoms, developmental delays, and metabolic acidosis, among other complications. Treatment typically involves dietary modifications, supplementation with specific nutrients, and, in some cases, enzyme replacement therapy.

Hexuronic acids are a type of uronic acid that contains six carbon atoms and is commonly found in various biological tissues and polysaccharides, such as pectins, heparin, and certain glycoproteins. The most common hexuronic acids are glucuronic acid and iduronic acid, which are formed from the oxidation of the corresponding hexoses, glucose and galactose, respectively. Hexuronic acids play important roles in various biological processes, including the detoxification and excretion of xenobiotics, the formation of proteoglycans, and the regulation of cell growth and differentiation.

The Electron Transport Chain (ETC) is a series of complexes in the inner mitochondrial membrane that are involved in the process of cellular respiration, through which the majority of energy is generated for the cell. The ETC complex proteins are a group of transmembrane protein complexes that facilitate the transfer of electrons from electron donors to electron acceptors via redox reactions. This transfer of electrons drives the generation of a proton gradient across the inner mitochondrial membrane, which is then used by ATP synthase to generate ATP, the primary energy currency of the cell.

The ETC complex proteins consist of four main complexes: Complex I (NADH-Q oxidoreductase), Complex II (succinate-Q oxidoreductase), Complex III (cytochrome bc1 complex or CoQ:cytochrome c oxidoreductase), and Complex IV (cytochrome c oxidase). Each complex contains a number of subunits, many of which are encoded by both the nuclear and mitochondrial genomes.

In summary, Electron Transport Chain Complex Proteins are a group of transmembrane protein complexes located in the inner mitochondrial membrane that facilitate the transfer of electrons from electron donors to electron acceptors, driving the generation of a proton gradient and ultimately ATP synthesis during cellular respiration.

Carbohydrate dehydrogenases are a group of enzymes that catalyze the oxidation of carbohydrates, including sugars and sugar alcohols. These enzymes play a crucial role in cellular metabolism by helping to convert these molecules into forms that can be used for energy or as building blocks for other biological compounds.

During the oxidation process, carbohydrate dehydrogenases remove hydrogen atoms from the carbohydrate substrate and transfer them to an electron acceptor, such as NAD+ or FAD. This results in the formation of a ketone or aldehyde group on the carbohydrate molecule and the reduction of the electron acceptor to NADH or FADH2.

Carbohydrate dehydrogenases are classified into several subgroups based on their substrate specificity, cofactor requirements, and other factors. Some examples include glucose dehydrogenase, galactose dehydrogenase, and sorbitol dehydrogenase.

These enzymes have important applications in various fields, including biotechnology, medicine, and industry. For example, they can be used to detect or quantify specific carbohydrates in biological samples, or to produce valuable chemical compounds through the oxidation of renewable resources such as plant-derived sugars.

Electron Spin Resonance (ESR) Spectroscopy, also known as Electron Paramagnetic Resonance (EPR) Spectroscopy, is a technique used to investigate materials with unpaired electrons. It is based on the principle of absorption of energy by the unpaired electrons when they are exposed to an external magnetic field and microwave radiation.

In this technique, a sample is placed in a magnetic field and microwave radiation is applied. The unpaired electrons in the sample absorb energy and change their spin state when the energy of the microwaves matches the energy difference between the spin states. This absorption of energy is recorded as a function of the magnetic field strength, producing an ESR spectrum.

ESR spectroscopy can provide information about the number, type, and behavior of unpaired electrons in a sample, as well as the local environment around the electron. It is widely used in physics, chemistry, and biology to study materials such as free radicals, transition metal ions, and defects in solids.

Resorcinols are a type of chemical compound that contain a resorcinol moiety, which is made up of a benzene ring with two hydroxyl groups in the ortho position. In medicine, resorcinol and its derivatives have been used for various purposes, including as antiseptics, antibacterials, and intermediates in the synthesis of other pharmaceuticals.

Resorcinol itself has some medicinal properties, such as being able to reduce pain and inflammation, and it has been used topically to treat conditions like eczema, psoriasis, and acne. However, resorcinol can also be toxic in large amounts, so it must be used with caution.

It's important to note that while resorcinol is a chemical compound, the term "resorcinols" may also refer to a group of related compounds that contain the resorcinol moiety. These compounds can have different medicinal properties and uses depending on their specific structure and function.

Dihydrolipoyllysine-residue acetyltransferase is a type of enzyme that plays a crucial role in the cellular process of energy production, specifically in the citric acid cycle (also known as the Krebs cycle or tricarboxylic acid cycle). This enzyme is responsible for transferring an acetyl group from acetyl-CoA to a specific residue on another protein called dihydrolipoyl dehydrogenase.

The reaction catalyzed by this enzyme can be summarized as follows:
Acetyl-CoA + dihydrolipoyl dehydrogenase (E3-DHLA) -> CoA + acetylated-dihydrolipoyl dehydrogenase (E3-DHLAA)

The acetylation of the dihydrolipoyl dehydrogenase protein is a necessary step in the citric acid cycle, which helps generate energy in the form of ATP through a series of oxidation-reduction reactions. Defects or mutations in this enzyme can lead to various metabolic disorders and diseases.

Metalloproteins are proteins that contain one or more metal ions as a cofactor, which is required for their biological activity. These metal ions play crucial roles in the catalytic function, structural stability, and electron transfer processes of metalloproteins. The types of metals involved can include iron, zinc, copper, magnesium, calcium, or manganese, among others. Examples of metalloproteins are hemoglobin (contains heme-bound iron), cytochrome c (contains heme-bound iron and functions in electron transfer), and carbonic anhydrase (contains zinc and catalyzes the conversion between carbon dioxide and bicarbonate).

Glucuronic acid is a physiological important organic acid, which is a derivative of glucose. It is formed by the oxidation of the primary alcohol group of glucose to form a carboxyl group at the sixth position. Glucuronic acid plays a crucial role in the detoxification process in the body as it conjugates with toxic substances, making them water-soluble and facilitating their excretion through urine or bile. This process is known as glucuronidation. It is also a component of various polysaccharides, such as heparan sulfate and chondroitin sulfate, which are found in the extracellular matrix of connective tissues.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Iron-sulfur proteins are a group of metalloproteins that contain iron and sulfur atoms in their active centers. These clusters of iron and sulfur atoms, also known as iron-sulfur clusters, can exist in various forms, including Fe-S, 2Fe-2S, 3Fe-4S, and 4Fe-4S structures. The iron atoms are coordinated to the protein through cysteine residues, while the sulfur atoms can be in the form of sulfide (S2-) or sulfane (-S-).

These proteins play crucial roles in many biological processes, such as electron transfer, redox reactions, and enzyme catalysis. They are found in various organisms, from bacteria to humans, and are involved in a wide range of cellular functions, including energy metabolism, photosynthesis, nitrogen fixation, and DNA repair.

Iron-sulfur proteins can be classified into several categories based on their structure and function, such as ferredoxins, Rieske proteins, high-potential iron-sulfur proteins (HiPIPs), and radical SAM enzymes. Dysregulation or mutations in iron-sulfur protein genes have been linked to various human diseases, including neurodegenerative disorders, cancer, and mitochondrial disorders.

Oxidation-Reduction (redox) reactions are a type of chemical reaction involving a transfer of electrons between two species. The substance that loses electrons in the reaction is oxidized, and the substance that gains electrons is reduced. Oxidation and reduction always occur together in a redox reaction, hence the term "oxidation-reduction."

In biological systems, redox reactions play a crucial role in many cellular processes, including energy production, metabolism, and signaling. The transfer of electrons in these reactions is often facilitated by specialized molecules called electron carriers, such as nicotinamide adenine dinucleotide (NAD+/NADH) and flavin adenine dinucleotide (FAD/FADH2).

The oxidation state of an element in a compound is a measure of the number of electrons that have been gained or lost relative to its neutral state. In redox reactions, the oxidation state of one or more elements changes as they gain or lose electrons. The substance that is oxidized has a higher oxidation state, while the substance that is reduced has a lower oxidation state.

Overall, oxidation-reduction reactions are fundamental to the functioning of living organisms and are involved in many important biological processes.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Flavoproteins are a type of protein molecule that contain noncovalently bound flavin mononucleotide (FMN) or flavin adenine dinucleotide (FAD) as cofactors. These flavin cofactors play a crucial role in redox reactions, acting as electron carriers in various metabolic pathways such as cellular respiration and oxidative phosphorylation. Flavoproteins are involved in several biological processes, including the breakdown of fatty acids, amino acids, and carbohydrates, as well as the synthesis of steroids and other lipids. They can also function as enzymes that catalyze various redox reactions, such as oxidases, dehydrogenases, and reductases. Flavoproteins are widely distributed in nature and found in many organisms, from bacteria to humans.

I'm sorry for any confusion, but "Hydrogen" is not a medical term. It is a chemical element with the symbol H and atomic number 1. It is the lightest and most abundant chemical element in the universe, making up about 75% of its elemental mass.

In a medical context, hydrogen can be discussed in terms of molecular hydrogen (H2) which has been studied for potential therapeutic benefits. Some research explores its use as an antioxidant and anti-inflammatory agent, but more studies are needed to confirm these effects and understand the mechanisms behind them.

Hydrogenase is not a medical term per se, but a biochemical term. It is used to describe an enzyme that catalyzes the reversible conversion between molecular hydrogen (H2) and protons (H+) or vice versa. These enzymes are found in certain bacteria, algae, and archaea, and they play a crucial role in their energy metabolism, particularly in processes like hydrogen production and consumption.

While not directly related to medical terminology, understanding the function of hydrogenase can be important in fields such as microbiology, molecular biology, and environmental science, which can have implications for human health in areas like infectious diseases, biofuels, and waste management.

In the context of medicine, iron is an essential micromineral and key component of various proteins and enzymes. It plays a crucial role in oxygen transport, DNA synthesis, and energy production within the body. Iron exists in two main forms: heme and non-heme. Heme iron is derived from hemoglobin and myoglobin in animal products, while non-heme iron comes from plant sources and supplements.

The recommended daily allowance (RDA) for iron varies depending on age, sex, and life stage:

* For men aged 19-50 years, the RDA is 8 mg/day
* For women aged 19-50 years, the RDA is 18 mg/day
* During pregnancy, the RDA increases to 27 mg/day
* During lactation, the RDA for breastfeeding mothers is 9 mg/day

Iron deficiency can lead to anemia, characterized by fatigue, weakness, and shortness of breath. Excessive iron intake may result in iron overload, causing damage to organs such as the liver and heart. Balanced iron levels are essential for maintaining optimal health.

Cytochromes are a type of hemeprotein found in the mitochondria and other cellular membranes of organisms. They contain a heme group, which is a prosthetic group composed of an iron atom surrounded by a porphyrin ring. This structure allows cytochromes to participate in redox reactions, acting as electron carriers in various biological processes.

There are several types of cytochromes, classified based on the type of heme they contain and their absorption spectra. Some of the most well-known cytochromes include:

* Cytochrome c: a small, mobile protein found in the inner mitochondrial membrane that plays a crucial role in the electron transport chain during cellular respiration.
* Cytochrome P450: a large family of enzymes involved in the metabolism of drugs, toxins, and other xenobiotics. They are found in various tissues, including the liver, lungs, and skin.
* Cytochrome b: a component of several electron transport chains, including those found in mitochondria, bacteria, and chloroplasts.

Cytochromes play essential roles in energy production, detoxification, and other metabolic processes, making them vital for the survival and function of living organisms.

Nitrogen is not typically referred to as a medical term, but it is an element that is crucial to medicine and human life.

In a medical context, nitrogen is often mentioned in relation to gas analysis, respiratory therapy, or medical gases. Nitrogen (N) is a colorless, odorless, and nonreactive gas that makes up about 78% of the Earth's atmosphere. It is an essential element for various biological processes, such as the growth and maintenance of organisms, because it is a key component of amino acids, nucleic acids, and other organic compounds.

In some medical applications, nitrogen is used to displace oxygen in a mixture to create a controlled environment with reduced oxygen levels (hypoxic conditions) for therapeutic purposes, such as in certain types of hyperbaric chambers. Additionally, nitrogen gas is sometimes used in cryotherapy, where extremely low temperatures are applied to tissues to reduce pain, swelling, and inflammation.

However, it's important to note that breathing pure nitrogen can be dangerous, as it can lead to unconsciousness and even death due to lack of oxygen (asphyxiation) within minutes.

Spectrophotometry is a technical analytical method used in the field of medicine and science to measure the amount of light absorbed or transmitted by a substance at specific wavelengths. This technique involves the use of a spectrophotometer, an instrument that measures the intensity of light as it passes through a sample.

In medical applications, spectrophotometry is often used in laboratory settings to analyze various biological samples such as blood, urine, and tissues. For example, it can be used to measure the concentration of specific chemicals or compounds in a sample by measuring the amount of light that is absorbed or transmitted at specific wavelengths.

In addition, spectrophotometry can also be used to assess the properties of biological tissues, such as their optical density and thickness. This information can be useful in the diagnosis and treatment of various medical conditions, including skin disorders, eye diseases, and cancer.

Overall, spectrophotometry is a valuable tool for medical professionals and researchers seeking to understand the composition and properties of various biological samples and tissues.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

The Ketoglutarate Dehydrogenase Complex (KGDC or α-KGDH) is a multi-enzyme complex that plays a crucial role in the Krebs cycle, also known as the citric acid cycle. It is located within the mitochondrial matrix of eukaryotic cells and functions to catalyze the oxidative decarboxylation of α-ketoglutarate into succinyl-CoA, thereby connecting the Krebs cycle to the electron transport chain for energy production.

The KGDC is composed of three distinct enzymes:

1. α-Ketoglutarate dehydrogenase (E1): This enzyme catalyzes the decarboxylation and oxidation of α-ketoglutarate to form a thioester intermediate with lipoamide, which is bound to the E2 component.
2. Dihydrolipoyl succinyltransferase (E2): This enzyme facilitates the transfer of the acetyl group from the lipoamide cofactor to CoA, forming succinyl-CoA and regenerating oxidized lipoamide.
3. Dihydrolipoyl dehydrogenase (E3): The final enzyme in the complex catalyzes the reoxidation of reduced lipoamide back to its disulfide form, using FAD as a cofactor and transferring electrons to NAD+, forming NADH.

The KGDC is subject to regulation by several mechanisms, including phosphorylation-dephosphorylation reactions that can inhibit or activate the complex, respectively. Dysfunction of this enzyme complex has been implicated in various diseases, such as neurodegenerative disorders and cancer.

"Klebsiella pneumoniae" is a medical term that refers to a type of bacteria belonging to the family Enterobacteriaceae. It's a gram-negative, encapsulated, non-motile, rod-shaped bacterium that can be found in various environments, including soil, water, and the gastrointestinal tracts of humans and animals.

"Klebsiella pneumoniae" is an opportunistic pathogen that can cause a range of infections, particularly in individuals with weakened immune systems or underlying medical conditions. It's a common cause of healthcare-associated infections, such as pneumonia, urinary tract infections, bloodstream infections, and wound infections.

The bacterium is known for its ability to produce a polysaccharide capsule that makes it resistant to phagocytosis by white blood cells, allowing it to evade the host's immune system. Additionally, "Klebsiella pneumoniae" has developed resistance to many antibiotics, making infections caused by this bacterium difficult to treat and a growing public health concern.

Dithionite is a chemical compound with the formula Na2S2O4. It is also known as sodium hydrosulfite or sodium dithionite. Dithionite is a white crystalline solid that is highly soluble in water and is commonly used as a reducing agent in various industrial and laboratory applications, including the reduction of iron and copper salts, the bleaching of textiles and pulp, and the removal of sulfur dioxide from flue gases.

In medical contexts, dithionite may be used as a reducing agent in some pharmaceutical preparations or as an antidote for certain types of poisoning. However, it is important to note that dithionite can be toxic and corrosive in concentrated forms, and should be handled with care.

Tricarboxylic acids, also known as TCA cycle or citric acid cycle, is a series of chemical reactions used by all living cells to generate energy through the oxidation of acetyl-CoA derived from carbohydrates, fats, and proteins into carbon dioxide and water in the form of ATP. This process is an important part of cellular respiration and occurs in the mitochondria. The cycle involves eight steps that result in the production of two molecules of ATP, reduced coenzymes NADH and FADH2, and the release of three molecules of carbon dioxide.

The tricarboxylic acids involved in this cycle are:

1. Citric acid (also known as citrate)
2. Cis-aconitic acid
3. Isocitric acid
4. Oxalosuccinic acid (an intermediate that is not regenerated)
5. α-Ketoglutaric acid (also known as alpha-ketoglutarate)
6. Succinyl-CoA
7. Succinic acid (also known as succinate)
8. Fumaric acid
9. Malic acid
10. Oxaloacetic acid (also known as oxalacetate)

These acids play a crucial role in the energy production and metabolism of living organisms.

'Escherichia coli' (E. coli) is a type of gram-negative, facultatively anaerobic, rod-shaped bacterium that commonly inhabits the intestinal tract of humans and warm-blooded animals. It is a member of the family Enterobacteriaceae and one of the most well-studied prokaryotic model organisms in molecular biology.

While most E. coli strains are harmless and even beneficial to their hosts, some serotypes can cause various forms of gastrointestinal and extraintestinal illnesses in humans and animals. These pathogenic strains possess virulence factors that enable them to colonize and damage host tissues, leading to diseases such as diarrhea, urinary tract infections, pneumonia, and sepsis.

E. coli is a versatile organism with remarkable genetic diversity, which allows it to adapt to various environmental niches. It can be found in water, soil, food, and various man-made environments, making it an essential indicator of fecal contamination and a common cause of foodborne illnesses. The study of E. coli has contributed significantly to our understanding of fundamental biological processes, including DNA replication, gene regulation, and protein synthesis.

Benzyl viologen is a type of chemical compound that belongs to the class of viologens, which are derivatives of the parent compound methylviologen. The chemical name for benzyl viologen is N,N'-diphenyl-4,4'-bipyridinium dichloride.

Viologens are reduced forms of heterocyclic aromatic amines that can undergo reversible reduction and oxidation reactions. In their reduced form, they act as strong reducing agents, while in their oxidized form, they act as strong oxidizing agents. Benzyl viologen is commonly used as an electron carrier or mediator in various chemical and biological systems, such as redox reactions, photochemical processes, and bioelectrochemical devices like fuel cells and biosensors.

The compound consists of two benzyl groups attached to the nitrogen atoms of a bipyridinium cation, which is then complexed with chloride ions. The reduction potential of benzyl viologen is around -0.45 V vs. standard hydrogen electrode (SHE), making it a useful electron carrier in various applications where an easily reducible and oxidizable compound is required.

It's worth noting that while benzyl viologen has potential uses in scientific research, it may also have toxic effects on living organisms, so appropriate safety precautions should be taken when handling this chemical.

Gene expression regulation in bacteria refers to the complex cellular processes that control the production of proteins from specific genes. This regulation allows bacteria to adapt to changing environmental conditions and ensure the appropriate amount of protein is produced at the right time.

Bacteria have a variety of mechanisms for regulating gene expression, including:

1. Operon structure: Many bacterial genes are organized into operons, which are clusters of genes that are transcribed together as a single mRNA molecule. The expression of these genes can be coordinately regulated by controlling the transcription of the entire operon.
2. Promoter regulation: Transcription is initiated at promoter regions upstream of the gene or operon. Bacteria have regulatory proteins called sigma factors that bind to the promoter and recruit RNA polymerase, the enzyme responsible for transcribing DNA into RNA. The binding of sigma factors can be influenced by environmental signals, allowing for regulation of transcription.
3. Attenuation: Some operons have regulatory regions called attenuators that control transcription termination. These regions contain hairpin structures that can form in the mRNA and cause transcription to stop prematurely. The formation of these hairpins is influenced by the concentration of specific metabolites, allowing for regulation of gene expression based on the availability of those metabolites.
4. Riboswitches: Some bacterial mRNAs contain regulatory elements called riboswitches that bind small molecules directly. When a small molecule binds to the riboswitch, it changes conformation and affects transcription or translation of the associated gene.
5. CRISPR-Cas systems: Bacteria use CRISPR-Cas systems for adaptive immunity against viruses and plasmids. These systems incorporate short sequences from foreign DNA into their own genome, which can then be used to recognize and cleave similar sequences in invading genetic elements.

Overall, gene expression regulation in bacteria is a complex process that allows them to respond quickly and efficiently to changing environmental conditions. Understanding these regulatory mechanisms can provide insights into bacterial physiology and help inform strategies for controlling bacterial growth and behavior.

Tetramethylphenylenediamine (TMPD) is not typically considered a medical term, but it is a chemical compound that is used in some scientific and research contexts. It's a type of aromatic amine, which is a class of organic compounds characterized by the presence of one or more amino groups (-NH2) attached to an aromatic hydrocarbon ring.

In biochemistry and molecular biology, TMPD is sometimes used as an electron carrier in experiments that involve redox reactions, such as those that occur during cellular respiration. It can also be used as a catalyst or reagent in various chemical reactions. However, it's important to note that TMPD is not a substance that is typically encountered in medical practice or patient care.

Protein conformation refers to the specific three-dimensional shape that a protein molecule assumes due to the spatial arrangement of its constituent amino acid residues and their associated chemical groups. This complex structure is determined by several factors, including covalent bonds (disulfide bridges), hydrogen bonds, van der Waals forces, and ionic bonds, which help stabilize the protein's unique conformation.

Protein conformations can be broadly classified into two categories: primary, secondary, tertiary, and quaternary structures. The primary structure represents the linear sequence of amino acids in a polypeptide chain. The secondary structure arises from local interactions between adjacent amino acid residues, leading to the formation of recurring motifs such as α-helices and β-sheets. Tertiary structure refers to the overall three-dimensional folding pattern of a single polypeptide chain, while quaternary structure describes the spatial arrangement of multiple folded polypeptide chains (subunits) that interact to form a functional protein complex.

Understanding protein conformation is crucial for elucidating protein function, as the specific three-dimensional shape of a protein directly influences its ability to interact with other molecules, such as ligands, nucleic acids, or other proteins. Any alterations in protein conformation due to genetic mutations, environmental factors, or chemical modifications can lead to loss of function, misfolding, aggregation, and disease states like neurodegenerative disorders and cancer.

2,6-Dichloroindophenol is a chemical compound that is used as an indicator in various analytical procedures, particularly in the field of biochemistry and microbiology. It is a derivative of indophenol, which contains two chlorine atoms at the 2nd and 6th positions of the benzene ring.

The chemical formula for 2,6-Dichloroindophenol is C8H6Cl2O2. This compound is a deep blue color in its oxidized state and turns colorless when reduced. The reduction potential of this compound makes it useful as an indicator in various redox reactions, including the determination of the concentration of reducing agents such as ascorbic acid (vitamin C) and other antioxidants.

It is important to note that 2,6-Dichloroindophenol is a hazardous chemical and should be handled with care. It can cause skin and eye irritation, and prolonged exposure may lead to more serious health effects. Therefore, it is essential to follow proper safety precautions when working with this compound.

Thulium is not a medical term, but a chemical element in the periodic table with atomic number 69. It's a rare earth metal that is silvery-gray and has a bright blue emission line in its spectrum. In medicine, thulium is used in some medical devices such as thulium lasers for the treatment of various conditions like kidney stones and benign prostatic hyperplasia (BPH). However, it's not a term that would be used to describe a medical condition or diagnosis.

Bacterial DNA refers to the genetic material found in bacteria. It is composed of a double-stranded helix containing four nucleotide bases - adenine (A), thymine (T), guanine (G), and cytosine (C) - that are linked together by phosphodiester bonds. The sequence of these bases in the DNA molecule carries the genetic information necessary for the growth, development, and reproduction of bacteria.

Bacterial DNA is circular in most bacterial species, although some have linear chromosomes. In addition to the main chromosome, many bacteria also contain small circular pieces of DNA called plasmids that can carry additional genes and provide resistance to antibiotics or other environmental stressors.

Unlike eukaryotic cells, which have their DNA enclosed within a nucleus, bacterial DNA is present in the cytoplasm of the cell, where it is in direct contact with the cell's metabolic machinery. This allows for rapid gene expression and regulation in response to changing environmental conditions.

The Electron Transport Chain (ETC) is a series of complexes in the inner mitochondrial membrane that are involved in the process of cellular respiration. It is the final pathway for electrons derived from the oxidation of nutrients such as glucose, fatty acids, and amino acids to be transferred to molecular oxygen. This transfer of electrons drives the generation of a proton gradient across the inner mitochondrial membrane, which is then used by ATP synthase to produce ATP, the main energy currency of the cell.

The electron transport chain consists of four complexes (I-IV) and two mobile electron carriers (ubiquinone and cytochrome c). Electrons from NADH and FADH2 are transferred to Complex I and Complex II respectively, which then pass them along to ubiquinone. Ubiquinone then transfers the electrons to Complex III, which passes them on to cytochrome c. Finally, cytochrome c transfers the electrons to Complex IV, where they combine with oxygen and protons to form water.

The transfer of electrons through the ETC is accompanied by the pumping of protons from the mitochondrial matrix to the intermembrane space, creating a proton gradient. The flow of protons back across the inner membrane through ATP synthase drives the synthesis of ATP from ADP and inorganic phosphate.

Overall, the electron transport chain is a crucial process for generating energy in the form of ATP in the cell, and it plays a key role in many metabolic pathways.

Alpha-ketoglutaric acid, also known as 2-oxoglutarate, is not an acid in the traditional sense but is instead a key molecule in the Krebs cycle (citric acid cycle), which is a central metabolic pathway involved in cellular respiration. Alpha-ketoglutaric acid is a crucial intermediate in the process of converting carbohydrates, fats, and proteins into energy through oxidation. It plays a vital role in amino acid synthesis and the breakdown of certain amino acids. Additionally, it serves as an essential cofactor for various enzymes involved in numerous biochemical reactions within the body. Any medical conditions or disorders related to alpha-ketoglutaric acid would typically be linked to metabolic dysfunctions or genetic defects affecting the Krebs cycle.

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

Non-heme iron proteins are a type of iron-containing protein that do not contain heme as their prosthetic group. Heme is a complex molecule consisting of an iron atom contained in the center of a porphyrin ring, which is a large organic molecule made up of four pyrrole rings joined together. In contrast, non-heme iron proteins contain iron that is bound to the protein in other ways, such as through coordination with amino acid side chains or through association with an iron-sulfur cluster.

Examples of non-heme iron proteins include ferritin and transferrin, which are involved in the storage and transport of iron in the body, respectively. Ferritin is a protein that stores iron in a form that is safe and bioavailable for use by the body. Transferrin, on the other hand, binds to iron in the intestines and transports it to cells throughout the body.

Non-heme iron proteins are important for many biological processes, including oxygen transport, electron transfer, and enzyme catalysis. They play a crucial role in energy metabolism, DNA synthesis, and other essential functions.

Ferricyanides are a class of chemical compounds that contain the ferricyanide ion (Fe(CN)6−3). The ferricyanide ion is composed of a central iron atom in the +3 oxidation state, surrounded by six cyanide ligands. Ferricyanides are strong oxidizing agents and are used in various chemical reactions, including analytical chemistry and as reagents in organic synthesis.

It's important to note that while ferricyanides themselves are not highly toxic, they can release cyanide ions if they are decomposed or reduced under certain conditions. Therefore, they should be handled with care and used in well-ventilated areas.

A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.

Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:

1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.

Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.

'Clostridium' is a genus of gram-positive, rod-shaped bacteria that are widely distributed in nature, including in soil, water, and the gastrointestinal tracts of animals and humans. Many species of Clostridium are anaerobic, meaning they can grow and reproduce in environments with little or no oxygen. Some species of Clostridium are capable of producing toxins that can cause serious and sometimes life-threatening illnesses in humans and animals.

Some notable species of Clostridium include:

* Clostridium tetani, which causes tetanus (also known as lockjaw)
* Clostridium botulinum, which produces botulinum toxin, the most potent neurotoxin known and the cause of botulism
* Clostridium difficile, which can cause severe diarrhea and colitis, particularly in people who have recently taken antibiotics
* Clostridium perfringens, which can cause food poisoning and gas gangrene.

It is important to note that not all species of Clostridium are harmful, and some are even beneficial, such as those used in the production of certain fermented foods like sauerkraut and natto. However, due to their ability to produce toxins and cause illness, it is important to handle and dispose of materials contaminated with Clostridium species carefully, especially in healthcare settings.

Quaternary ammonium compounds (QACs) are a group of disinfectants and antiseptics that contain a nitrogen atom surrounded by four organic groups, resulting in a charged "quat" structure. They are widely used in healthcare settings due to their broad-spectrum activity against bacteria, viruses, fungi, and spores. QACs work by disrupting the cell membrane of microorganisms, leading to their death. Common examples include benzalkonium chloride and cetyltrimethylammonium bromide. It is important to note that some microorganisms have developed resistance to QACs, and they may not be effective against all types of pathogens.

Flavin-Adenine Dinucleotide (FAD) is a coenzyme that plays a crucial role in various metabolic processes, particularly in the electron transport chain where it functions as an electron carrier in oxidation-reduction reactions. FAD is composed of a flavin moiety, riboflavin or vitamin B2, and adenine dinucleotide. It can exist in two forms: an oxidized form (FAD) and a reduced form (FADH2). The reduction of FAD to FADH2 involves the gain of two electrons and two protons, which is accompanied by a significant conformational change that allows FADH2 to donate its electrons to subsequent components in the electron transport chain, ultimately leading to the production of ATP, the main energy currency of the cell.

Culture media is a substance that is used to support the growth of microorganisms or cells in an artificial environment, such as a petri dish or test tube. It typically contains nutrients and other factors that are necessary for the growth and survival of the organisms being cultured. There are many different types of culture media, each with its own specific formulation and intended use. Some common examples include blood agar, which is used to culture bacteria; Sabouraud dextrose agar, which is used to culture fungi; and Eagle's minimum essential medium, which is used to culture animal cells.

Acetyltransferases are a type of enzyme that facilitates the transfer of an acetyl group (a chemical group consisting of an acetyl molecule, which is made up of carbon, hydrogen, and oxygen atoms) from a donor molecule to a recipient molecule. This transfer of an acetyl group can modify the function or activity of the recipient molecule.

In the context of biology and medicine, acetyltransferases are important for various cellular processes, including gene expression, DNA replication, and protein function. For example, histone acetyltransferases (HATs) are a type of acetyltransferase that add an acetyl group to the histone proteins around which DNA is wound. This modification can alter the structure of the chromatin, making certain genes more or less accessible for transcription, and thereby influencing gene expression.

Abnormal regulation of acetyltransferases has been implicated in various diseases, including cancer, neurodegenerative disorders, and infectious diseases. Therefore, understanding the function and regulation of these enzymes is an important area of research in biomedicine.

Potentiometry is a method used in analytical chemistry to measure the potential (or voltage) difference between two electrodes, which reflects the concentration of an ion or a particular molecule in a solution. It involves setting up an electrochemical cell with two electrodes: a working electrode and a reference electrode. The working electrode is immersed in the test solution and its potential is measured against the stable potential of the reference electrode.

The Nernst equation can be used to relate the potential difference to the concentration of the analyte, allowing for quantitative analysis. Potentiometry is often used to measure the activity or concentration of ions such as H+, Na+, K+, and Cl-, as well as other redox-active species.

In medical testing, potentiometry can be used to measure the concentration of certain ions in biological fluids such as blood, urine, or sweat. For example, it can be used to measure the pH of a solution (the concentration of H+ ions) or the concentration of glucose in blood using a glucometer.

Methylphenazonium methosulfate is not a medication itself, but rather a reagent used in the production and pharmacological research of certain medications. It's commonly used as a redox mediator, which means it helps to facilitate electron transfer in chemical reactions. In medical contexts, it may be used in the laboratory synthesis or testing of some drugs.

It's important to note that methylphenazonium methosulfate is not intended for direct medical use in humans or animals. Always consult with a healthcare professional or trusted medical source for information regarding specific medications and their uses.

Sulfur is not typically referred to in the context of a medical definition, as it is an element found in nature and not a specific medical condition or concept. However, sulfur does have some relevance to certain medical topics:

* Sulfur is an essential element that is a component of several amino acids (the building blocks of proteins) and is necessary for the proper functioning of enzymes and other biological processes in the body.
* Sulfur-containing compounds, such as glutathione, play important roles in antioxidant defense and detoxification in the body.
* Some medications and supplements contain sulfur or sulfur-containing compounds, such as dimethyl sulfoxide (DMSO), which is used topically for pain relief and inflammation.
* Sulfur baths and other forms of sulfur-based therapies have been used historically in alternative medicine to treat various conditions, although their effectiveness is not well-established by scientific research.

It's important to note that while sulfur itself is not a medical term, it can be relevant to certain medical topics and should be discussed with a healthcare professional if you have any questions or concerns about its use in medications, supplements, or therapies.

Adenosine Triphosphate (ATP) is a high-energy molecule that stores and transports energy within cells. It is the main source of energy for most cellular processes, including muscle contraction, nerve impulse transmission, and protein synthesis. ATP is composed of a base (adenine), a sugar (ribose), and three phosphate groups. The bonds between these phosphate groups contain a significant amount of energy, which can be released when the bond between the second and third phosphate group is broken, resulting in the formation of adenosine diphosphate (ADP) and inorganic phosphate. This process is known as hydrolysis and can be catalyzed by various enzymes to drive a wide range of cellular functions. ATP can also be regenerated from ADP through various metabolic pathways, such as oxidative phosphorylation or substrate-level phosphorylation, allowing for the continuous supply of energy to cells.

Ferredoxin-NADP Reductase (FDNR) is an enzyme that catalyzes the electron transfer from ferredoxin to NADP+, reducing it to NADPH. This reaction plays a crucial role in several metabolic pathways, including photosynthesis and nitrogen fixation.

In photosynthesis, FDNR is located in the stroma of chloroplasts and receives electrons from ferredoxin, which is reduced by photosystem I. The enzyme then transfers these electrons to NADP+, generating NADPH, which is used in the Calvin cycle for carbon fixation.

In nitrogen fixation, FDNR is found in the nitrogen-fixing bacteria and receives electrons from ferredoxin, which is reduced by nitrogenase. The enzyme then transfers these electrons to NADP+, generating NADPH, which is used in the reduction of nitrogen gas (N2) to ammonia (NH3).

FDNR is a flavoprotein that contains a FAD cofactor and an iron-sulfur cluster. The enzyme catalyzes the electron transfer through a series of conformational changes that bring ferredoxin and NADP+ in close proximity, allowing for efficient electron transfer.

Cyanides are a group of chemical compounds that contain the cyano group, -CN, which consists of a carbon atom triple-bonded to a nitrogen atom. They are highly toxic and can cause rapid death due to the inhibition of cellular respiration. Cyanide ions (CN-) bind to the ferric iron in cytochrome c oxidase, a crucial enzyme in the electron transport chain, preventing the flow of electrons and the production of ATP, leading to cellular asphyxiation.

Common sources of cyanides include industrial chemicals such as hydrogen cyanide (HCN) and potassium cyanide (KCN), as well as natural sources like certain fruits, nuts, and plants. Exposure to high levels of cyanides can occur through inhalation, ingestion, or skin absorption, leading to symptoms such as headache, dizziness, nausea, vomiting, rapid heartbeat, seizures, coma, and ultimately death. Treatment for cyanide poisoning typically involves the use of antidotes that bind to cyanide ions and convert them into less toxic forms, such as thiosulfate and rhodanese.

I'm sorry for any confusion, but "Polyesters" is not a medical term. It is a term used in materials science and textile industry to describe a type of synthetic fiber made from polymers characterized by the presence of ester groups in their main chain. If you have any questions related to medical terminology or concepts, I'd be happy to help with those instead!

Apoproteins are the protein components of lipoprotein complexes, which are responsible for transporting fat molecules, such as cholesterol and triglycerides, throughout the body. Apoproteins play a crucial role in the metabolism of lipids by acting as recognition signals that allow lipoproteins to interact with specific receptors on cell surfaces.

There are several different types of apoproteins, each with distinct functions. For example, apolipoprotein A-1 (apoA-1) is the major protein component of high-density lipoproteins (HDL), which are responsible for transporting excess cholesterol from tissues to the liver for excretion. Apolipoprotein B (apoB) is a large apoprotein found in low-density lipoproteins (LDL), very low-density lipoproteins (VLDL), and lipoprotein(a). ApoB plays a critical role in the assembly and secretion of VLDL from the liver, and it also mediates the uptake of LDL by cells.

Abnormalities in apoprotein levels or function can contribute to the development of various diseases, including cardiovascular disease, diabetes, and Alzheimer's disease. Therefore, measuring apoprotein levels in the blood can provide valuable information for diagnosing and monitoring these conditions.

Potassium Cyanide (C6H5KN) is defined as a white, water-soluble, crystalline salt that is highly toxic. It is used in fumigation, electroplating, and metal cleaning. When combined with acids, it releases the deadly gas hydrogen cyanide. It can cause immediate death by inhibiting cellular respiration. It is also known as Cyanide of Potassium or Potassium Salt of Hydrocyanic Acid.

Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.

I'm sorry for any confusion, but "spectrum analysis" is not a commonly used medical term. Spectrum analysis is a term that is more frequently used in the fields of physics, mathematics, and engineering to describe the process of breaking down a signal or a wave into its different frequencies and amplitudes, creating a visual representation called a spectrum.

If you have any concerns about a medical issue, I would recommend consulting with a healthcare professional for accurate information and guidance.

Magnetic Resonance Spectroscopy (MRS) is a non-invasive diagnostic technique that provides information about the biochemical composition of tissues, including their metabolic state. It is often used in conjunction with Magnetic Resonance Imaging (MRI) to analyze various metabolites within body tissues, such as the brain, heart, liver, and muscles.

During MRS, a strong magnetic field, radio waves, and a computer are used to produce detailed images and data about the concentration of specific metabolites in the targeted tissue or organ. This technique can help detect abnormalities related to energy metabolism, neurotransmitter levels, pH balance, and other biochemical processes, which can be useful for diagnosing and monitoring various medical conditions, including cancer, neurological disorders, and metabolic diseases.

There are different types of MRS, such as Proton (^1^H) MRS, Phosphorus-31 (^31^P) MRS, and Carbon-13 (^13^C) MRS, each focusing on specific elements or metabolites within the body. The choice of MRS technique depends on the clinical question being addressed and the type of information needed for diagnosis or monitoring purposes.

"Rhodospirillum rubrum" is a gram-negative, facultatively anaerobic, photosynthetic bacteria species. It is commonly found in freshwater and soil environments, and it has the ability to carry out both photosynthesis and respiration, depending on the availability of light and oxygen. The bacteria contain bacteriochlorophyll and carotenoid pigments, which give them a pinkish-red color, hence the name "rubrum." They are known to be important organisms in the study of photosynthesis, nitrogen fixation, and other metabolic processes.

Oxygen is a colorless, odorless, tasteless gas that constitutes about 21% of the earth's atmosphere. It is a crucial element for human and most living organisms as it is vital for respiration. Inhaled oxygen enters the lungs and binds to hemoglobin in red blood cells, which carries it to tissues throughout the body where it is used to convert nutrients into energy and carbon dioxide, a waste product that is exhaled.

Medically, supplemental oxygen therapy may be provided to patients with conditions such as chronic obstructive pulmonary disease (COPD), pneumonia, heart failure, or other medical conditions that impair the body's ability to extract sufficient oxygen from the air. Oxygen can be administered through various devices, including nasal cannulas, face masks, and ventilators.

PII nitrogen regulatory proteins are a type of signal transduction protein involved in the regulation of nitrogen metabolism in bacteria and archaea. They are named "PII" because they contain two identical subunits, each with a molecular weight of approximately 12 kilodaltons. These proteins play a crucial role in sensing and responding to changes in the energy status and nitrogen availability within the cell.

The PII protein is composed of three domains: the T-domain, which binds ATP and ADP; the N-domain, which binds 2-oxoglutarate (an indicator of carbon and nitrogen status); and the B-domain, which is involved in signal transduction. The PII protein can exist in different conformational states depending on whether it is bound to ATP or ADP, and this affects its ability to interact with downstream effectors.

One of the primary functions of PII proteins is to regulate the activity of glutamine synthetase (GS), an enzyme that catalyzes the conversion of glutamate to glutamine. When nitrogen is abundant, PII proteins bind to GS and stimulate its activity, promoting the assimilation of ammonia into organic compounds. Conversely, when nitrogen is scarce, PII proteins dissociate from GS, allowing it to be inhibited by other regulatory proteins.

PII proteins can also interact with other enzymes and regulators involved in nitrogen metabolism, such as nitrogenase, uridylyltransferase/uridylyl-removing enzyme (UT/UR), and transcriptional regulators. Through these interactions, PII proteins help to coordinate the cell's response to changes in nitrogen availability and energy status, ensuring that resources are allocated efficiently and effectively.

Adenosine diphosphate (ADP) is a chemical compound that plays a crucial role in energy transfer within cells. It is a nucleotide, which consists of a adenosine molecule (a sugar molecule called ribose attached to a nitrogenous base called adenine) and two phosphate groups.

In the cell, ADP functions as an intermediate in the conversion of energy from one form to another. When a high-energy phosphate bond in ADP is broken, energy is released and ADP is converted to adenosine triphosphate (ATP), which serves as the main energy currency of the cell. Conversely, when ATP donates a phosphate group to another molecule, it is converted back to ADP, releasing energy for the cell to use.

ADP also plays a role in blood clotting and other physiological processes. In the coagulation cascade, ADP released from damaged red blood cells can help activate platelets and initiate the formation of a blood clot.

Hydrogen-ion concentration, also known as pH, is a measure of the acidity or basicity of a solution. It is defined as the negative logarithm (to the base 10) of the hydrogen ion activity in a solution. The standard unit of measurement is the pH unit. A pH of 7 is neutral, less than 7 is acidic, and greater than 7 is basic.

In medical terms, hydrogen-ion concentration is important for maintaining homeostasis within the body. For example, in the stomach, a high hydrogen-ion concentration (low pH) is necessary for the digestion of food. However, in other parts of the body such as blood, a high hydrogen-ion concentration can be harmful and lead to acidosis. Conversely, a low hydrogen-ion concentration (high pH) in the blood can lead to alkalosis. Both acidosis and alkalosis can have serious consequences on various organ systems if not corrected.

Circular dichroism (CD) is a technique used in physics and chemistry to study the structure of molecules, particularly large biological molecules such as proteins and nucleic acids. It measures the difference in absorption of left-handed and right-handed circularly polarized light by a sample. This difference in absorption can provide information about the three-dimensional structure of the molecule, including its chirality or "handedness."

In more technical terms, CD is a form of spectroscopy that measures the differential absorption of left and right circularly polarized light as a function of wavelength. The CD signal is measured in units of millidegrees (mdeg) and can be positive or negative, depending on the type of chromophore and its orientation within the molecule.

CD spectra can provide valuable information about the secondary and tertiary structure of proteins, as well as the conformation of nucleic acids. For example, alpha-helical proteins typically exhibit a strong positive band near 190 nm and two negative bands at around 208 nm and 222 nm, while beta-sheet proteins show a strong positive band near 195 nm and two negative bands at around 217 nm and 175 nm.

CD spectroscopy is a powerful tool for studying the structural changes that occur in biological molecules under different conditions, such as temperature, pH, or the presence of ligands or other molecules. It can also be used to monitor the folding and unfolding of proteins, as well as the binding of drugs or other small molecules to their targets.

Spectrophotometry, Ultraviolet (UV-Vis) is a type of spectrophotometry that measures how much ultraviolet (UV) and visible light is absorbed or transmitted by a sample. It uses a device called a spectrophotometer to measure the intensity of light at different wavelengths as it passes through a sample. The resulting data can be used to determine the concentration of specific components within the sample, identify unknown substances, or evaluate the physical and chemical properties of materials.

UV-Vis spectroscopy is widely used in various fields such as chemistry, biology, pharmaceuticals, and environmental science. It can detect a wide range of substances including organic compounds, metal ions, proteins, nucleic acids, and dyes. The technique is non-destructive, meaning that the sample remains unchanged after the measurement.

In UV-Vis spectroscopy, the sample is placed in a cuvette or other container, and light from a source is directed through it. The light then passes through a monochromator, which separates it into its component wavelengths. The monochromatic light is then directed through the sample, and the intensity of the transmitted or absorbed light is measured by a detector.

The resulting absorption spectrum can provide information about the concentration and identity of the components in the sample. For example, if a compound has a known absorption maximum at a specific wavelength, its concentration can be determined by measuring the absorbance at that wavelength and comparing it to a standard curve.

Overall, UV-Vis spectrophotometry is a versatile and powerful analytical technique for quantitative and qualitative analysis of various samples in different fields.

Ammonia is a colorless, pungent-smelling gas with the chemical formula NH3. It is a compound of nitrogen and hydrogen and is a basic compound, meaning it has a pH greater than 7. Ammonia is naturally found in the environment and is produced by the breakdown of organic matter, such as animal waste and decomposing plants. In the medical field, ammonia is most commonly discussed in relation to its role in human metabolism and its potential toxicity.

In the body, ammonia is produced as a byproduct of protein metabolism and is typically converted to urea in the liver and excreted in the urine. However, if the liver is not functioning properly or if there is an excess of protein in the diet, ammonia can accumulate in the blood and cause a condition called hyperammonemia. Hyperammonemia can lead to serious neurological symptoms, such as confusion, seizures, and coma, and is treated by lowering the level of ammonia in the blood through medications, dietary changes, and dialysis.

Nitrate reductase is an enzyme that catalyzes the reduction of nitrate (NO3-) to nitrite (NO2-). It is widely distributed in nature and plays a crucial role in the nitrogen cycle, particularly in the process of nitrate assimilation by plants, fungi, and some bacteria.

In plants, nitrate reductase is primarily located in the cytoplasm and chloroplasts of plant cells. It requires reduced forms of nicotinamide adenine dinucleotide phosphate (NADPH) or flavin adenine dinucleotide (FADH2) as electron donors to facilitate the reduction of nitrate to nitrite.

The reaction catalyzed by nitrate reductase can be summarized as follows:
NO3- + NAD(P)H + H+ -> NO2- + NAD(P)+ + H2O

It is worth noting that there are different types of nitrate reductases, each with distinct properties and functions. For example, some nitrate reductases require molybdenum cofactor as a prosthetic group for their catalytic activity, while others do not. Additionally, some nitrate reductases are membrane-bound, while others are soluble enzymes.

Overall, nitrate reductase is an essential enzyme in the global nitrogen cycle and has significant implications for agriculture, environmental science, and microbiology.

Acetates, in a medical context, most commonly refer to compounds that contain the acetate group, which is an functional group consisting of a carbon atom bonded to two hydrogen atoms and an oxygen atom (-COO-). An example of an acetate is sodium acetate (CH3COONa), which is a salt formed from acetic acid (CH3COOH) and is often used as a buffering agent in medical solutions.

Acetates can also refer to a group of medications that contain acetate as an active ingredient, such as magnesium acetate, which is used as a laxative, or calcium acetate, which is used to treat high levels of phosphate in the blood.

In addition, acetates can also refer to a process called acetylation, which is the addition of an acetyl group (-COCH3) to a molecule. This process can be important in the metabolism and regulation of various substances within the body.

Glutamate-ammonia ligase, also known as glutamine synthetase, is an enzyme that plays a crucial role in nitrogen metabolism. It catalyzes the formation of glutamine from glutamate and ammonia in the presence of ATP, resulting in the conversion of ammonia to a less toxic form. This reaction is essential for maintaining nitrogen balance in the body and for the synthesis of various amino acids, nucleotides, and other biomolecules. The enzyme is widely distributed in various tissues, including the brain, liver, and muscle, and its activity is tightly regulated through feedback inhibition by glutamine and other metabolites.

Site-directed mutagenesis is a molecular biology technique used to introduce specific and targeted changes to a specific DNA sequence. This process involves creating a new variant of a gene or a specific region of interest within a DNA molecule by introducing a planned, deliberate change, or mutation, at a predetermined site within the DNA sequence.

The methodology typically involves the use of molecular tools such as PCR (polymerase chain reaction), restriction enzymes, and/or ligases to introduce the desired mutation(s) into a plasmid or other vector containing the target DNA sequence. The resulting modified DNA molecule can then be used to transform host cells, allowing for the production of large quantities of the mutated gene or protein for further study.

Site-directed mutagenesis is a valuable tool in basic research, drug discovery, and biotechnology applications where specific changes to a DNA sequence are required to understand gene function, investigate protein structure/function relationships, or engineer novel biological properties into existing genes or proteins.

Mössbauer spectroscopy is a nuclear solid-state physics technique that provides detailed information about the chemical environment and electronic structure of iron (Fe), tin (Sn), antimony (Sb), and other nuclei in a sample. This technique uses the Mössbauer effect, which is the recoil-free emission and absorption of gamma rays by atomic nuclei bound in a solid lattice.

In Mössbauer spectroscopy, a source emits gamma rays that are absorbed by atoms with the same nuclear species in the sample. The energy of the gamma rays can be shifted due to the interaction between the gamma rays and the atomic electrons, which is influenced by the chemical environment and electronic structure of the nuclei in the sample. By analyzing these shifts in energy, researchers can determine various properties of the sample, such as oxidation state, coordination number, and local symmetry around the absorbing nuclei.

Mössbauer spectroscopy is a valuable tool for studying materials with high resolution and sensitivity to subtle changes in their structure and composition. It has applications in fields such as chemistry, physics, biology, geology, and materials science.

A plasmid is a small, circular, double-stranded DNA molecule that is separate from the chromosomal DNA of a bacterium or other organism. Plasmids are typically not essential for the survival of the organism, but they can confer beneficial traits such as antibiotic resistance or the ability to degrade certain types of pollutants.

Plasmids are capable of replicating independently of the chromosomal DNA and can be transferred between bacteria through a process called conjugation. They often contain genes that provide resistance to antibiotics, heavy metals, and other environmental stressors. Plasmids have also been engineered for use in molecular biology as cloning vectors, allowing scientists to replicate and manipulate specific DNA sequences.

Plasmids are important tools in genetic engineering and biotechnology because they can be easily manipulated and transferred between organisms. They have been used to produce vaccines, diagnostic tests, and genetically modified organisms (GMOs) for various applications, including agriculture, medicine, and industry.

Carbon-sulfur lyases are a class of enzymes that catalyze the cleavage of carbon-sulfur bonds in organic compounds, resulting in the formation of a new double bond. These enzymes play important roles in various biological processes, including the metabolism of sulfur-containing amino acids and the biosynthesis of certain cofactors and secondary metabolites.

Carbon-sulfur lyases are classified under EC number 4.4.1, which includes enzymes that catalyze the formation of carbon-carbon bonds by means other than those involving oxidoreductases. Within this class, carbon-sulfur lyases are further divided into several subcategories based on their specific reaction mechanisms and substrate specificities.

One example of a carbon-sulfur lyase is cysteine desulfurase (EC 2.8.1.7), which catalyzes the formation of alanine and a persulfide group from L-cysteine, releasing elemental sulfur as a byproduct. This enzyme plays a critical role in the biosynthesis of iron-sulfur clusters, which are essential cofactors for many proteins involved in electron transfer reactions.

Another example is 3-mercaptopyruvate sulfurtransferase (EC 2.8.1.2), which catalyzes the formation of a persulfide group on a cysteine residue in the enzyme itself, using 3-mercaptopyruvate as a sulfur donor. This enzyme is involved in the biosynthesis of various secondary metabolites containing sulfur atoms, such as allicin in garlic and penicillamine in certain fungi.

Overall, carbon-sulfur lyases are important enzymes that play critical roles in various biological processes involving the cleavage or formation of carbon-sulfur bonds.

Methylamines are organic compounds that contain a methyl group (CH3) and an amino group (-NH2). They have the general formula of CH3-NH-R, where R can be a hydrogen atom or any organic group. Methylamines are derivatives of ammonia (NH3), in which one or more hydrogen atoms have been replaced by methyl groups.

There are several types of methylamines, including:

1. Methylamine (CH3-NH2): This is the simplest methylamine and is a colorless gas at room temperature with a strong odor. It is highly flammable and reactive.
2. Dimethylamine (CH3)2-NH: This is a colorless liquid at room temperature with an unpleasant fishy odor. It is less reactive than methylamine but still highly flammable.
3. Trimethylamine (CH3)3-N: This is a colorless liquid at room temperature that has a strong, unpleasant odor often described as "fishy." It is less reactive than dimethylamine and is used in various industrial applications.

Methylamines are used in the production of various chemicals, including pesticides, dyes, and pharmaceuticals. They can also be found naturally in some foods and are produced by certain types of bacteria in the body. Exposure to high levels of methylamines can cause irritation to the eyes, skin, and respiratory tract, and prolonged exposure can lead to more serious health effects.

Macromolecular substances, also known as macromolecules, are large, complex molecules made up of repeating subunits called monomers. These substances are formed through polymerization, a process in which many small molecules combine to form a larger one. Macromolecular substances can be naturally occurring, such as proteins, DNA, and carbohydrates, or synthetic, such as plastics and synthetic fibers.

In the context of medicine, macromolecular substances are often used in the development of drugs and medical devices. For example, some drugs are designed to bind to specific macromolecules in the body, such as proteins or DNA, in order to alter their function and produce a therapeutic effect. Additionally, macromolecular substances may be used in the creation of medical implants, such as artificial joints and heart valves, due to their strength and durability.

It is important for healthcare professionals to have an understanding of macromolecular substances and how they function in the body, as this knowledge can inform the development and use of medical treatments.

"Chromatium" is a genus of bacteria that are commonly found in aquatic environments, particularly in anaerobic or low-oxygen conditions. These bacteria are known for their ability to perform anaerobic respiration using sulfur as the final electron acceptor in the electron transport chain. This process is often referred to as "sulfur reduction" or "sulfur respiration."

The name "Chromatium" comes from the Greek word "chroma," which means "color," and refers to the distinctive purple color of these bacteria, which is due to the presence of bacteriochlorophyll and carotenoid pigments. These pigments allow Chromatium species to perform photosynthesis, using light energy to convert carbon dioxide into organic compounds.

It's worth noting that "Chromatium" is a specific taxonomic name for a genus of bacteria, and should not be confused with the more general term "chromatin," which refers to the complex of DNA, histone proteins, and other molecules that make up the chromosomes in eukaryotic cells.

Restriction mapping is a technique used in molecular biology to identify the location and arrangement of specific restriction endonuclease recognition sites within a DNA molecule. Restriction endonucleases are enzymes that cut double-stranded DNA at specific sequences, producing fragments of various lengths. By digesting the DNA with different combinations of these enzymes and analyzing the resulting fragment sizes through techniques such as agarose gel electrophoresis, researchers can generate a restriction map - a visual representation of the locations and distances between recognition sites on the DNA molecule. This information is crucial for various applications, including cloning, genome analysis, and genetic engineering.

In the context of medicine, "chemistry" often refers to the field of study concerned with the properties, composition, and structure of elements and compounds, as well as their reactions with one another. It is a fundamental science that underlies much of modern medicine, including pharmacology (the study of drugs), toxicology (the study of poisons), and biochemistry (the study of the chemical processes that occur within living organisms).

In addition to its role as a basic science, chemistry is also used in medical testing and diagnosis. For example, clinical chemistry involves the analysis of bodily fluids such as blood and urine to detect and measure various substances, such as glucose, cholesterol, and electrolytes, that can provide important information about a person's health status.

Overall, chemistry plays a critical role in understanding the mechanisms of diseases, developing new treatments, and improving diagnostic tests and techniques.

Oxygen consumption, also known as oxygen uptake, is the amount of oxygen that is consumed or utilized by the body during a specific period of time, usually measured in liters per minute (L/min). It is a common measurement used in exercise physiology and critical care medicine to assess an individual's aerobic metabolism and overall health status.

In clinical settings, oxygen consumption is often measured during cardiopulmonary exercise testing (CPET) to evaluate cardiovascular function, pulmonary function, and exercise capacity in patients with various medical conditions such as heart failure, chronic obstructive pulmonary disease (COPD), and other respiratory or cardiac disorders.

During exercise, oxygen is consumed by the muscles to generate energy through a process called oxidative phosphorylation. The amount of oxygen consumed during exercise can provide important information about an individual's fitness level, exercise capacity, and overall health status. Additionally, measuring oxygen consumption can help healthcare providers assess the effectiveness of treatments and rehabilitation programs in patients with various medical conditions.

An operon is a genetic unit in prokaryotic organisms (like bacteria) consisting of a cluster of genes that are transcribed together as a single mRNA molecule, which then undergoes translation to produce multiple proteins. This genetic organization allows for the coordinated regulation of genes that are involved in the same metabolic pathway or functional process. The unit typically includes promoter and operator regions that control the transcription of the operon, as well as structural genes encoding the proteins. Operons were first discovered in bacteria, but similar genetic organizations have been found in some eukaryotic organisms, such as yeast.

Molecular weight, also known as molecular mass, is the mass of a molecule. It is expressed in units of atomic mass units (amu) or daltons (Da). Molecular weight is calculated by adding up the atomic weights of each atom in a molecule. It is a useful property in chemistry and biology, as it can be used to determine the concentration of a substance in a solution, or to calculate the amount of a substance that will react with another in a chemical reaction.

Sulfurtransferases are a group of enzymes that catalyze the transfer of a sulfur group from one molecule to another. These enzymes play a crucial role in various biological processes, including the detoxification of harmful compounds and the synthesis of important metabolites. They can be found in many organisms, from bacteria to humans.

In humans, there are several types of sulfurtransferases, including cysteine conjugate beta-lyase, rhodanese, and 3'-phosphoadenosine 5'-phosphosulfate (PAPS) reductase. These enzymes have different substrates and functions, but they all share the ability to transfer a sulfur group from one molecule to another.

For example, rhodanese is an enzyme that transfers a sulfur atom from thiosulfate to cyanide, converting it to less toxic thiocyanate. This reaction is important in the detoxification of cyanide in the body.

Sulfurtransferases are also involved in the synthesis of various metabolites, such as iron-sulfur clusters and molybdenum cofactor, which are essential for the function of many enzymes.

Deficiencies or mutations in sulfurtransferase genes can lead to various diseases and disorders, highlighting their importance in human health.

Chemical phenomena refer to the changes and interactions that occur at the molecular or atomic level when chemicals are involved. These phenomena can include chemical reactions, in which one or more substances (reactants) are converted into different substances (products), as well as physical properties that change as a result of chemical interactions, such as color, state of matter, and solubility. Chemical phenomena can be studied through various scientific disciplines, including chemistry, biochemistry, and physics.

Molecular models are three-dimensional representations of molecular structures that are used in the field of molecular biology and chemistry to visualize and understand the spatial arrangement of atoms and bonds within a molecule. These models can be physical or computer-generated and allow researchers to study the shape, size, and behavior of molecules, which is crucial for understanding their function and interactions with other molecules.

Physical molecular models are often made up of balls (representing atoms) connected by rods or sticks (representing bonds). These models can be constructed manually using materials such as plastic or wooden balls and rods, or they can be created using 3D printing technology.

Computer-generated molecular models, on the other hand, are created using specialized software that allows researchers to visualize and manipulate molecular structures in three dimensions. These models can be used to simulate molecular interactions, predict molecular behavior, and design new drugs or chemicals with specific properties. Overall, molecular models play a critical role in advancing our understanding of molecular structures and their functions.

Flavin Mononucleotide (FMN) is a coenzyme that plays a crucial role in biological oxidation-reduction reactions. It is derived from the vitamin riboflavin (also known as vitamin B2) and is composed of a flavin molecule bonded to a nucleotide. FMN functions as an electron carrier, accepting and donating electrons in various metabolic pathways, including the citric acid cycle and the electron transport chain, which are essential for energy production in cells. It also participates in the detoxification of harmful substances and contributes to the maintenance of cellular redox homeostasis. FMN can exist in two forms: the oxidized form (FMN) and the reduced form (FMNH2), depending on its involvement in redox reactions.

Bacterial transformation is a natural process by which exogenous DNA is taken up and incorporated into the genome of a bacterial cell. This process was first discovered in 1928 by Frederick Griffith, who observed that dead virulent bacteria could transfer genetic material to live avirulent bacteria, thereby conferring new properties such as virulence to the recipient cells.

The uptake of DNA by bacterial cells typically occurs through a process called "competence," which can be either naturally induced under certain environmental conditions or artificially induced in the laboratory using various methods. Once inside the cell, the exogenous DNA may undergo recombination with the host genome, resulting in the acquisition of new genes or the alteration of existing ones.

Bacterial transformation has important implications for both basic research and biotechnology. It is a powerful tool for studying gene function and for engineering bacteria with novel properties, such as the ability to produce valuable proteins or degrade environmental pollutants. However, it also poses potential risks in the context of genetic engineering and biocontainment, as transformed bacteria may be able to transfer their newly acquired genes to other organisms in the environment.

... Genome Project Current research on Azotobacter vinelandii at the Norwich Research Park Type strain of ... Azotobacter vinelandii is Gram-negative diazotroph that can fix nitrogen while grown aerobically. These bacteria are easily ... Nagpal P, Jafri S, Reddy MA, Das HK (1989). "Multiple chromosomes of Azotobacter vinelandii". J. Bacteriol. 171 (6): 3133-8. ... Maldonado R, Jiménez J, Casadesús J (1994). "Changes of ploidy during the Azotobacter vinelandii growth cycle" (PDF). J. ...
"Azotobacter.org". Archived from the original (A project to study the genome of Azotobacter vinelandii) on 20 May 2013. ... In 1909, Lipman described Azotobacter vinelandii, and a year later Azotobacter beijerinckii Lipman, 1904, which he named in ... "Azotobacter vinelandii". JGI. Archived from the original on 2009-07-03. Iwao WATANABE (JICA/Cantho Univ. Expert Mar-Apr. 2000 ... "Azotobacter vinelandii". John Innes Centre - Molecular Microbiology Department. Archived from the original on 2014-02-19. ...
Maldonado R, Jiménez J, Casadesús J (July 1994). "Changes of ploidy during the Azotobacter vinelandii growth cycle". Journal of ... Nagpal P, Jafri S, Reddy MA, Das HK (June 1989). "Multiple chromosomes of Azotobacter vinelandii". Journal of Bacteriology. 171 ... Azotobacter vinelandii can contain up to 80 chromosome copies per cell. However this is only observed in fast growing cultures ...
Heppel LA, Hurwitz J, Horecker BL (1957). "Adenine deaminase of Azotobacter vinelandii". J. Am. Chem. Soc. 79 (3): 630-633. doi ...
I. Polynucleotide phosphorylase of azotobacter vinelandii". Biochimica et Biophysica Acta. 20 (1): 269-85. doi:10.1016/0006- ...
Azotobacter vinelandii is a nitrogen-fixing bacteria which is known by its high respiratory rate among aerobic organisms. Some ... The cytochrome system of Azotobacter vinelandii. Biochim Biophys Acta. 1967 Sep 6;143(2):340-353 (Cytochromes). ...
"Azotobacter vinelandii: a Pseudomonas in disguise?". Microbiology. 150 (Pt 5): 1117-9. doi:10.1099/mic.0.27096-0. PMID 15133068 ... ISBN 978-1-904455-19-6. Young, J. M.; Park, D. -C. (2007). "Probable synonymy of the nitrogen-fixing genus Azotobacter and the ... The nitrogen-fixing bacteria of the genus Azotobacter and the species Azomonas macrocytogenes have evolved from a species in ... Its nitrogen-fixing capabilities and deviant features have caused Azotobacter to be described as "Pseudomonas in disguise". The ...
I. Polynucleotide phosphorylase of Azotobacter vinelandii". Biochimica et Biophysica Acta. 20 (1): 269-85. doi:10.1016/0006- ...
Homologous ferredoxins from Azotobacter vinelandii (Av2FeFdI; P82802) and Aquifex aeolicus (AaFd; O66511) have been ... August 2017). "The Electron Bifurcating FixABCX Protein Complex from Azotobacter vinelandii: Generation of Low-Potential ... "Discovery of a novel ferredoxin from Azotobacter vinelandii containing two [4Fe-4S] clusters with widely differing and very ... In Azotobacter the energy released by transferring one electron from NADH to Q is used to simultaneously boost the transfer of ...
Rediers, H; Vanderleyden, J; De Mot, R (2004). "Azotobacter vinelandii: a Pseudomonas in disguise?". Microbiology. 150 (Pt 5): ... Young, J. M.; Park, D. -C. (2007). "Probable synonymy of the nitrogen-fixing genus Azotobacter and the genus Pseudomonas". ... In the gammaproteobacterial order Pseudomonadales, the genus Azotobacter and the species Azomonas macrocytogenes are actually ...
"Azotobacter vinelandii: a Pseudomonas in disguise?". Microbiology. 150 (Pt 5): 1117-9. doi:10.1099/mic.0.27096-0. PMID 15133068 ... Kennedy C, Rudnick P, MacDonald ML, Melton T (2015). "Azotobacter". Bergey's Manual of Systematics of Archaea and Bacteria. pp ... The Pseudomonadaceae are a family of bacteria which includes the genera Azomonas, Azorhizophilus, Azotobacter, Mesophilobacter ...
doi:10.2138/rmg.2005.59.4. Huyer M, Page WJ (1988). "Zn2+ Increases Siderophore Production in Azotobacter vinelandii". Applied ...
Davidson IW, Lawson CJ, Sutherland IW (January 1977). "An alginate lysate from Azotobacter vinelandii phage". Journal of ...
Azotobacter vinelandii is the most studied of these organisms. It uses very high respiration rates, and protective compounds, ... Two of the most studied systems are those of Klebsiella pneumoniae and Azotobacter vinelandii. These systems are studied ... Marine Nitrogen Fixation - The Basics (USC Capone Lab) Azotobacter Rhizobia Frankia & Actinorhizal Plants (CS1 maint: multiple ... Diazotroph biofertilizers used today include Rhizobium, Azotobacter, Azospirilium and Blue green algae (a genus of ...
Burgess BK, Jacobs DB, Stiefel EI (July 1980). "Large-scale purification of high activity Azotobacter vinelandII nitrogenase". ...
Imai T (January 1973). "Purification and properties of nicotinamide mononucleotide amidohydrolase from Azotobacter vinelandii ...
Strandberg, G. W.; Wilson, P. W. (1968). "Formation of the nitrogen-fixing enzyme system in Azotobacter vinelandii". Canadian ...
The Anf nitrogenase in Azotobacter vinelandii is organized in an anfHDGKOR operon. This operon still requires some of the Nif ... of MgATP and MgADP interaction with the nitrogenase of Azotobacter vinelandii. Lysine 15 of the iron protein plays a major role ... "Mössbauer Study of the MoFe Protein of Nitrogenase from Azotobacter vinelandii Using Selective 57Fe Enrichment of the M-Centers ... "Evidence for a central role of lysine 15 of Azotobacter vinelandii nitrogenase iron protein in nucleotide binding and protein ...
Azotobacter vinelandii, obligate aerobe diazotroph used in nitrogen fixation research. Streptomyces coelicolor, soil-dwelling ...
acetan (Acetobacter xylinum) alginate (Azotobacter vinelandii) cellulose (Acetobacter xylinum) chitosan (Mucorales spp.) ...
... is structurally similar to azobactin, from Azotobacter vinelandii, except that the latter possesses an extra urea ... "Characterization of the pyoverdines of Azotobacter vinelandii ATCC 12837 with regard to heterogeneity". Biology of Metals. 4 (4 ...
... new pathway for resorcinol catabolism in Azotobacter vinelandii". J. Bacteriol. 146 (2): 460-6. PMC 216987. PMID 7217008. ...
The cubic core structure, found in species such as Azotobacter vinelandii, is made up of 24 subunits total. The catalytic ... structure of the dihydrolipoyl transacetylase component of the pyruvate dehydrogenase complex from Azotobacter vinelandii. A ...
The phenolic lipid synthesis by type III polyketide synthases is essential for cyst formation in Azotobacter vinelandii. Lipid ... "Phenolic lipid synthesis by type III polyketide synthases is essential for cyst formation in Azotobacter vinelandii". ...
Azotobacter vinelandii". Bioscience, Biotechnology, and Biochemistry. 66 (3): 489-500. doi:10.1271/bbb.66.489. PMID 12005040. ...
... she demonstrated cell free protein synthesis with a particulate preparation from Azotobacter vinelandii. She did her post- ...
... from Azotobacter chroococcum and comparison of its redox potentials with those of flavodoxins from Azotobacter vinelandii and ... "Regulation of nitrogen fixation in Klebsiella pneumoniae and Azotobacter vinelandii: NifL, transducing two environmental ...
The following values are from Azotobacter vinelandii (1): KM: 0.14 ± 0.04 mM Vmax : 9 ± 3 μmol.min−1.mg−1 The reaction ... "Kinetic properties of the 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii evidence for the formation of a ...
... as well as the related Azotobacter vinelandii. They are consistently located in what could be the 5' untranslated regions of ...
The candidates have been Acidithiobacillus thiooxidans (discovered in NJ, 1922), Azotobacter vinelandii (discovered in Vineland ...
Azotobacter vinelandii Genome Project Current research on Azotobacter vinelandii at the Norwich Research Park Type strain of ... Azotobacter vinelandii is Gram-negative diazotroph that can fix nitrogen while grown aerobically. These bacteria are easily ... Nagpal P, Jafri S, Reddy MA, Das HK (1989). "Multiple chromosomes of Azotobacter vinelandii". J. Bacteriol. 171 (6): 3133-8. ... Maldonado R, Jiménez J, Casadesús J (1994). "Changes of ploidy during the Azotobacter vinelandii growth cycle" (PDF). J. ...
keywords = "algae, azotobacter, Azotobacter vinelandii, carbon, fluxomic analysis",. author = "Lieve Laurens and Chao Wu and ... In this study, we used Azotobacter vinelandii DJ and an ammonium excreting mutant, AV3 (..delta..NifL), to investigate central ... In this study, we used Azotobacter vinelandii DJ and an ammonium excreting mutant, AV3 (..delta..NifL), to investigate central ... In this study, we used Azotobacter vinelandii DJ and an ammonium excreting mutant, AV3 (..delta..NifL), to investigate central ...
Species Azotobacter vinelandii [TaxId:354] [52662] (15 PDB entries). *. Domain d2afhe1: 2afh E:1-289 [126683]. Other proteins ... d2afhe1 c.37.1.10 (E:1-289) Nitrogenase iron protein {Azotobacter vinelandii [TaxId: 354]} ...
Effective results for Azotobacter vinelandii DJ (eggnog40). Summary. Number of putative secreted proteins: 221 - Predicted by ...
Dinitrogenase - Nitrogenase Links: Kalottenmodell der Nitrogenase von Azotobacter vinelandii (stabilisiert) nach PDB … Deutsch ... Azotobacter spp.). An important source of nitrogen in unfertilized… … Glossary of Biotechnology ...
Azotobacter vinelandii Using Azotobacter vinelandii on your plants and soil can lead to enhanced nitrogen availability, ... Azotobacter-(multiple species). Azotobacter(multiple strains) fixes atmospheric nitrogen for all plant types. Has one of the ... Azotobacter chroococcum. Using Azotobacter chroococcum on your plants and soil can significantly enhance plant growth by fixing ... From Azotobacter to Bacillus and Rhizobium to Mycorrhizal Fungi, each component plays a crucial role in creating a healthy soil ...
Several aspects of alginate and PHB synthesis in Azotobacter vinelandii at a molecular level have been elucidated in articles ... Molecular and bioengineering strategies to improve alginate and polydydroxyalkanoate production by Azotobacter vinelandii ...
Azotobacter vinelandii. AhpC like peroxiredoxin. complete. Nicolas Rouhier. 4918. AxAhpC Firmicutes. Amphibacillus xylanus. ...
Azotobacter vinelandii DJ Bacteria normal 1 n/a -. NC_008740 Maqu_1726 phage integrase family protein 30.2 ...
gi,226942170,ref,NC_012560.1,:3699059-3699991 Azotobacter vinelandii DJ chromosome, complete genome. ... gi,226945684,ref,YP_002800757.1, unnamed protein product [Azotobacter vinelandii DJ]. ...
Host Lineage: Azotobacter vinelandii; Azotobacter; Pseudomonadaceae; Pseudomonadales; Proteobacteria; Bacteria. General ... Azotobacter vinelandii also produces a number of unusual nitrogenases which allow it to fix atmospheric nitrogen to ammonia, a ... Query: NC_021150:1823874:1826837 Azotobacter vinelandii CA6, complete genome. Start: 1826837, End: 1827376, Length: 540. ... Azotobacter vinelandii DJ, complete genome. transcriptional regulator, TetR family. 4e-101. 366. ...
Rault-Leonardon, M., Atkinson, M.A., Slaughter, C.A., Moomaw, C.R. and Srere, P.A. (1995). „Azotobacter vinelandii citrate ...
Azotobacter vinelandii); CAE49913 (Corynebacterium diphtheriae); NP_625531 (Streptomyces coelicolor); YP_144848 (Thermus ...
Azotobacter vinelandii (4) * Asma (3) * Baço (2) * Queimaduras (2) * Cateterismo de Swan-Ganz (2) ...
Amares® is a Azotobacter Vinelandii.. Natural bacterial preparation that will directly impact the health of crops.. For new and ...
A. vinelandii ATCC12518 and Azotobacter sp. strain (CCT) previously isolated were used for biochemical identification and ... In addition, all Azotobacter species have the capacity to produce oxidases and catalases for the protection of their ... It has been reported that Azotobacter has the capacity to produce soluble pigments (1, 4), this can be a useful tool in the ... On the other hand, it is necessary to design species-specific primers for the genus Azotobacter because of its large importance ...
Cytokinins in Azotobacter vinelandii culture medium. Appl Environ Microbiol. 1989;55(1):266-267.. Crossref ... Biosynthesis of cytokinins by Azotobacter chroococcum. Soil Biol Biochem. 1989;21(7):967-972.. Crossref ... Potential involvement of plant-growth promoting rhizobacteria (PGPR) like Azospirillum, Azotobacter, Bacillus, Pseudomonas spp ...
Safety in numbers: multiple occurrences of highly similar homologs among Azotobacter vinelandii carbohydrate metabolism ...
C1DQG8 phosphate acetyltransferase (EC 2.3.1.8) from Azotobacter vinelandii. 712 amino acids: PaperBLAST, CDD 71% identical to ... C1DER7 phosphate acetyltransferase (EC 2.3.1.8) from Azotobacter vinelandii. 691 amino acids: PaperBLAST, CDD 70% identical to ...
Expression and content of terminal oxidases in Azotobacter vinelandii grown with excess NH4+ are modulated by O-2 supply. ... Expression and content of terminal oxidases in Azotobacter vinelandii grown with excess NH4+ are modulated by O-2 supply. ...
"The In Vivo Potential-Regulated Protective Protein of Nitrogenase in Azotobacter vinelandii Supports Aerobic Bioelectrochemical ...
... using molecular replacement phases derived from the structure of the catalytic domain from the Azotobacter vinelandii ... vinelandii E2pCD 24mer. Like E2pCD and chloramphenicol acetyltransferase (CAT), the active site of E2oCD is located in the ...
Biofertilizant Rhizosum N 50 gr Acest biofertilizant contine bacteria Azotobacter vinelandii si alte microorganisme rizosferice ...
Leonardite, Arthobacter globiformis, Azospirillum brasilense, A.lipoferum, Azotobacter chrooccum, A.paspali, A.vinelandii, ... Leonardite, Arthobacter globiformis, Azospirillum brasilense, A.lipoferum, Azotobacter chrooccum, A.paspali, A.vinelandii, ... Leonardite, Pea Protein, Arthobacter globiformis, Azospirillum brasilense, A.lipoferum, Azotobacter chroococcum, A.paspali, A. ... Leonardite, Pea Protein, Arthobacter globiformis, Azospirillum brasilense, A.lipoferum, Azotobacter chroococcum, A.paspali, A. ...
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Involvement Of Azotobacter Vinelandii Hypothetical Protein Avin_16040 In Oryza Sativa Root Attachment by: Pauline, Liew Woan ...
Effect of iron limitation on the isotopic composition of cellular and released fixed nitrogen in Azotobacter vinelandii ...
Suzbijanje patogene gljive Botrytis cinerea na vinovoj lozi benefitnim gljivama Trichoderma harzianum i Trichoderma vinelandii ... Uloga nitrofiksirajućih bakterija Azotobacter spp. i Azospirillum spp. u biljnoj proizvodnji. Ravnjak, Boris ...
  • The nitrogenase holoenzyme of A. vinelandii has been characterised by X-ray crystallography in both ADP tetrafluoroaluminate-bound and MgATP-bound states. (wikipedia.org)
  • Using Azotobacter chroococcum on your plants and soil can significantly enhance plant growth by fixing atmospheric nitrogen, making it readily available for plant uptake. (sonoagfertilizer.com)
  • Micronoc is an OMRI listed dry seed treatment meticulously crafted with multiple strains of rhizobium, bacillus, and azotobacter, combined in a humate powder. (sonoagfertilizer.com)
  • From Azotobacter to Bacillus and Rhizobium to Mycorrhizal Fungi, each component plays a crucial role in creating a healthy soil ecosystem. (sonoagfertilizer.com)
  • Unlike Azotobacter, Rhizobium is dependent on a plant relationship. (sonoagfertilizer.com)
  • Azotobacter vinelandii is Gram-negative diazotroph that can fix nitrogen while grown aerobically. (wikipedia.org)
  • Azotobacter(multiple strains) fixes atmospheric nitrogen for all plant types. (sonoagfertilizer.com)
  • Azotobacter vinelandii also produces a number of unusual nitrogenases which allow it to fix atmospheric nitrogen to ammonia, a compound it can then use as a nitrogen source. (up.ac.za)
  • With the purpose of isolating and characterizing free nitrogen fixing bacteria (FNFB) of the genus Azotobacter, soil samples were collected randomly from different vegetable organic cultures with neutral pH in different zones of Boyacá-Colombia. (loveisnotlostinnovations.com)
  • A. vinelandii can contain up to 80 chromosome copies per cell. (wikipedia.org)
  • In this work we demonstrated the utility of molecular techniques and bioinformatics tools as a support to conventional techniques in characterization of the genus Azotobacter from vegetable-grown soils. (loveisnotlostinnovations.com)
  • A. vinelandii is a free-living N2 fixer known to produce many phytohormones and vitamins in soils. (wikipedia.org)
  • The MoFe protein component from Azotobacter vinelandii OP. (nih.gov)
  • nifB- MoFe protein (nifB-Av1), ΔnifE MoFe protein (ΔnifE Av1) and ΔnifZ MoFe protein ΔnifZ Av1) were obtained by chromatography on DE52, Sephacryl S-300 and Q-Sepharose columns from nifB point-mutated, nifE deleted and nifZ deleted mutant stains (UW45, DJ35 and DJ194) of Azotobacter vinelandii Lipmann, respectively. (jipb.net)