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.
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)
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 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)
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.
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.
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 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)
Salts of alginic acid that are extracted from marine kelp and used to make dental impressions and as absorbent material for surgical dressings.
Proteins that have one or more tightly bound metal ions forming part of their structure. (Dorland, 28th ed)
Enzymes that catalyze the epimerization of chiral centers within carbohydrates or their derivatives. EC 5.1.3.
The functional hereditary units of BACTERIA.
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.
Proteins found in any species of bacterium.
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)
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 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.
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)
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.
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 transfer of the planetary sulfur atom of thiosulfate ion to cyanide ion to form thiocyanate ion. EC 2.8.1.1.
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).
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.
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.
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.
Dithionite. The dithionous acid ion and its salts.
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 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.
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.
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 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.
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 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.
The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.
Gram-negative, non-motile, capsulated, gas-producing rods found widely in nature and associated with urinary and respiratory infections in humans.
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.
The rate dynamics in chemical or physical systems.
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.
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.
Proteins, usually acting in oxidation-reduction reactions, containing iron but no porphyrin groups. (Lehninger, Principles of Biochemistry, 1993, pG-10)

Cloning and expression of the algL gene, encoding the Azotobacter chroococcum alginate lyase: purification and characterization of the enzyme. (1/423)

The alginate lyase-encoding gene (algL) of Azotobacter chroococcum was localized to a 3.1-kb EcoRI DNA fragment that revealed an open reading frame of 1,116 bp. This open reading frame encodes a protein of 42.98 kDa, in agreement with the value previously reported by us for this protein. The deduced protein has a potential N-terminal signal peptide that is consistent with its proposed periplasmic location. The analysis of the deduced amino acid sequence indicated that the gene sequence has a high homology (90% identity) to the Azotobacter vinelandii gene sequence, which has very recently been deposited in the GenBank database, and that it has 64% identity to the Pseudomonas aeruginosa gene sequence but that it has rather low homology (15 to 22% identity) to the gene sequences encoding alginate lyase in other bacteria. The A. chroococcum AlgL protein was overproduced in Escherichia coli and purified to electrophoretic homogeneity in a two-step chromatography procedure on hydroxyapatite and phenyl-Sepharose. The kinetic and molecular parameters of the recombinant alginate lyase are similar to those found for the native enzyme.  (+info)

Flavodoxin: an allosteric inhibitor of AMP nucleosidase from Azotobacter vinelandii. (2/423)

Flavodoxin, which participates in nitrogen fixation, was found to be a potent allosteric inhibitor of AMP nucleosidase [EC 3.2.2.4] from Azotobacter vinelandii. It inhibited the enzyme by decreasing its affinity for ATP without affecting the maximum velocity. The inhibition constant for flavodoxin was estimated to be 10 muM, which is within the range of physiological concentration in the cells. The concentration of flavodoxin able to alter the activity in vitro suggests that this phenomenon could be of significance in the regulation of flavin biosynthesis in vivo. Flavin mononucleotide (FMN), a prosthetic group of flavodoxin, was also found to act as an allosteric inhibitor. Since no inhibitory action of apo-flavodoxin was observed, it was concluded that the FMN chromophore of the flavodoxin is responsible for the inhibition of the enzyme by this protein.  (+info)

Interactions of heterologous nitrogenase components that generate catalytically inactive complexes. (3/423)

A unique method is described for inhibiting nitrogenase. When Clostridium pasteurianum nitrogenase is assayed in the presence of the Mo-Fe protein of Azotobacter vinelandii, all the characteristic activities of nitrogenase are inhibited. C. pasteurianum nitrogenase is unaffected by the Fe protein of A. vinelandii. The Fe protein, but not the Mo-Fe protein of C. pasteurianum, inhibits A. vinelandii nitrogenase. Both inhibitions described result from the formation of an inactive complex of A. vinelandii Mo-Fe protein and C. pasteurianum Fe protein. Complex formation requires active components, as oxygen-denatured proteins are ineffective. The results for titration of components of the complex against each other and kinetic data each indicate that the inactive complex consists of two molecules of C. pasteurianum Fe protein per molecule of A. vinelandii Mo-Fe protein. The results of kinetic experiments suggest that the Fe protein from each organism competes for the same site(s) on the A. vinelandii Mo-Fe protein. The Fe protein of C. pasteurianum will form an active or an inactive complex with the Mo-Fe proteins from six different organisms. Inhibition by nitrogenase components that form inactive complexes provides numeroius ways to study the mechanism of nitrogenase action.  (+info)

Transcription of bacteriophage deoxyribonucleic acid. Comparison of Escherichia coli and Azotobacter vinelandii sigma subunits. (4/423)

The effect of the sigma subunit of RNA polymerase on the rate and asymmetry of the in vitro transcription of Escherichia coli and Azotobacter vinelandii phage DNAs has been studied with purified E. coli and A. vinelandii RNA polymerases and hybrid enzymes containing the core subunits of one enzyme and sigma from the other. The effect of sigma on the rate of transcription is characteristic of the template and not of the enzyme and depends on ionic strength. The rate of transcription of A. vinelandii phage A21 DNA is decreased by sigma at high ionic strength, but shows the more characteristic stimulation at KCl concentrations below 0.05 M. In contrast, the stimulation by sigma of T4 DNA transcription increased with an increase in the KCl concentrations. All combinations of core and sigma subunits behaved similarly with respect to stimulation or inhibition by sigma and with respect to asymmetric transcription of S13 replicative form (RF)DNA. However, the heterologous, but not the homologous combinations of core and sigma transcribed A21 symmetrically. S13 RF DNA in the superhelical, but not in the relaxed configuration, is transcribed asymmetrically by the A. vinelandii core enzyme. A role for the core subunits in specific site recognition is indicated by this observation.  (+info)

Transcription of Azotobacter phage deoxyribonucleic acid. Salt-dependent equilibrium between steps in initiation. (5/423)

The transcription of Azotobacter phage A21 DNA by Escherichia coli or Azotobacter vinelandii RNA polymerase differs from that of some other DNAs in its inhibition by moderate concentrations of KCl. This characteristic results in an apparent low template activity for this DNA as compared with T4 DNA under standard assay conditions. From an analysis of the dependence of the various steps in initiation on KCl it is concluded that the effect is exerted on an equilibrium between an inactive polymerase-DNA complex and an active preintitiation complex. This salt-sensitive equilibrium favors the inactive complex at a lower KCl concentration than with other templates. It can be approached from other low or high salt concentrations at a measurably slow rate.  (+info)

Evidence for a two-electron transfer using the all-ferrous Fe protein during nitrogenase catalysis. (6/423)

The nitrogenase-catalyzed H(2) evolution and acetylene-reduction reactions using Ti(III) and dithionite (DT) as reductants were examined and compared under a variety of conditions. Ti(III) is known to make the all-ferrous Fe protein ([Fe(4)S(4)](0)) and lowers the amount of ATP hydrolyzed during nitrogenase catalysis by approximately 2-fold. Here we further investigate this behavior and present results consistent with the Fe protein in the [Fe(4)S(4)](0) redox state transferring two electrons ([Fe(4)S(4)](2+)/[Fe(4)S(4)](0)) per MoFe protein interaction using Ti(III) but transferring only one electron ([Fe(4)S(4)](2+)/[Fe(4)S(4)](1+)) using DT. MoFe protein specific activity was measured as a function of Fe:MoFe protein ratio for both a one- and a two-electron transfer reaction, and nearly identical curves were obtained. However, Fe protein specific activity curves as a function of MoFe:Fe protein ratio showed two distinct reactivity patterns. With DT as reductant, typical MoFe inhibition curves were obtained for operation of the [Fe(4)S(4)](2+)/[Fe(4)S(4)](1+) redox couple, but with Ti(III) as reductant the [Fe(4)S(4)](2+)/[Fe(4)S(4)](0) redox couple was functional and MoFe inhibition was not observed at high MoFe:Fe protein ratios. With Ti(III) as reductant, nitrogenase catalysis produced hyperbolic curves, yielding a V(max) for the Fe protein specific activity of about 3200 nmol of H(2) min(-1) mg(-1) Fe protein, significantly higher than for reactions conducted with DT as reductant. Lag phase experiments (Hageman, R. V., and Burris, R. H. (1978) Proc. Natl. Acad. Sci. U. S. A. 75, 2699-2702) were carried out at MoFe:Fe protein ratios of 100 and 300 using both DT and Ti(III). A lag phase was observed for DT but, with Ti(III) product formation, began immediately and remained linear for over 30 min. Activity measurements using Av-Cp heterologous crosses were examined using both DT and Ti(III) as reductants to compare the reactivity of the [Fe(4)S(4)](2+)/[Fe(4)S(4)](1+) and [Fe(4)S(4)](2+)/[Fe(4)S(4)](0) redox couples and both were inactive. The results are discussed in terms of the Fe protein transferring two electrons per MoFe protein encounter using the [Fe(4)S(4)](2+)/[Fe(4)S(4)](0) redox couple with Ti(III) as reductant.  (+info)

Purification and properties of nitrogenase from the cyanobacterium, Anabaena cylindrica. (7/423)

The nitrogenase complex was isolated from nitrogen-starved cultures of Anabaema cylindrica. Sodium dithionite, photochemically reduced ferredoxin, and NADPH were found to be effective election donors to nitro genase in crude extracts whereas hydrogen and pyruvate were not. The Km for acetylene in vivo is ten-fold higher than the Km in vitro, whereas this pattern does not hold for the non-heterocystous cyanobacterium, Plectonema boryanum. This indicates that at least one mechanism of oxygen protection in vivo involves a gas diffusion barrier presented by the heterocyst cell wall. The Mo-Fe component was purified to homogeneity. Its molecular weight (220,000), subunit composition, isoelectric point (4.8), Mo, Fe, and S2- content (2, 20 and 20 mol/mol component), and amino acid composition indicate that this component has similar properties to Mo-Fe-containing components isolated from other bacterial sources. The isolated components from A. cylindrica were found to cross-react, to varying degrees, with components isolated from Azotobacter vinelandii, Rhodospirillum rubrum, and P. boryanum.  (+info)

Studies on the product binding sites of the Azotobacter vinelandii ribonucleic acid polymerase. (8/423)

During chain elongation RNA polymerase exists as a ternary DNA-enzyme-RNA complex in which a discrete length of the nascent RNA chain proximal to the 3'-OH terminus will be bound to the product binding site (Krakow, J. S., and Fronk, E. (1969) J. Biol. Chem. 244, 5988). We have utilized the poly[d(A-T)]-directed reaction to determine the length of the nascent poly[r(A-U)] protected from attack by pancreatic ribonuclease. Following release of the ribonuclease resistant oligo[r(A-U)] from the ternary complex, its size was determined by ion exchange chromatography on DEAE-cellulose, gel filtration on Bio-Gel P-10, and the ratio of 3'-terminal uridine to internal 2':3'-UMP following alkaline hydrolysis. The results indicate that the length of the nascent protected fragment is approximately 12 residues.  (+info)

'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.

'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.

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.

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!

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.

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.

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.

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.

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.

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).

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

"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.

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 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.

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.

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.

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.

In dry soils, Azotobacter can survive in the form of cysts for up to 24 years. Representatives of the genus Azotobacter are ... "Azotobacter.org". Archived from the original (A project to study the genome of Azotobacter vinelandii) on 20 May 2013. ... nigricans and Azotobacter nigricans subsp. achromogenes; in the same year, Thompson and Skerman described Azotobacter ... "Azotobacter". Euzéby, J. P. "Azotobacter Beijerinck 1901". List of Prokaryotic names with Standing in Nomenclature. " ...
Unlike other Azotobacter species, iron was absolutely required for growth. While most Azotobacter species are commonly found in ... "ITIS Standard Report Page: Azotobacter Salinestris." ITIS Standard Report Page: Azotobacter Salinestris. N.p., 1991. Web. 8 Feb ... Prokaryote Wikispecies has information related to Azotobacter salinestris. Portal: Biology Parte, A.C. "Azotobacter". LPSN. ... Azotobacter salinestris is a Gram-negative, rod-shaped organism. This organism's cells are about 2 x 4 μm in size when they are ...
... 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 ... "Why it is possible to reduce Nitrogen fertilizers by using Azotobacter sp". Retrieved 14 June 2018. Requena N, Baca TM, Azcon R ... Nagpal P, Jafri S, Reddy MA, Das HK (1989). "Multiple chromosomes of Azotobacter vinelandii". J. Bacteriol. 171 (6): 3133-8. ...
Type strain of Azotobacter chroococcum at BacDive - the Bacterial Diversity Metadatabase v t e (CS1 German-language sources (de ... Azotobacter chroococcum is a bacterium that has the ability to fix atmospheric nitrogen. It was discovered by Martinus ... Parte, A.C. "Azotobacter". LPSN. Beijerinck M. W. (1901). "Ueber Oligonitrophile Mikroben". Zentralblatt für Bakteriologie, ... Wani, Sartaj; Chand, Subhash; Ali, Tahir (29 August 2013). "Potential Use of Azotobacter chroococcum in Crop Production: An ...
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 ... "Azotobacter vinelandii: a Pseudomonas in disguise?". Microbiology. 150 (Pt 5): 1117-9. doi:10.1099/mic.0.27096-0. PMID 15133068 ...
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For example, the Azotobacter sp. degrades 2,4,6-trichlorophenol (2,4,6-TCP) into 2,6-dichlorohydroquinone due to TCP-4- ... Other species such as Pseudomonas galthei or Azotobacter sp. showed preference for para-halide over the meta- or ortho -halides ...
... s are found in members of the bacterial genus Azotobacter as well as the species Rhodopseudomonas palustris ... Miller R. W.; Eady R. R. (1988). "Molybdenum and vanadium nitrogenases of Azotobacter chroococcum. Low temperature favours N2 ... Eady R. R. (1989). "The Vanadium Nitrogenase of Azotobacter". Polyhedron. 8 (13/14): 1695-1700. doi:10.1016/S0277-5387(00)80619 ...
Krasil'nikov NA (1949). "Is Azotobacter present in lichens?". Mikrobiologiia. 18: 3. Lambright, DD Kapustka, LA (1981). "The ...
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 ...
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Wyss, Orville; Neumann, Marilyn G.; Socolofsky, M. D. (1961). "Development and Germination of the Azotobacter Cyst". The ... Vela, G. R.; Wyss, Orville (1964). "Improved Stain for Visualization of Azotobacter Encystment". Journal of Bacteriology. 87 (2 ... Vela, Gerard R.; Wyss, Orville (1965). "Radiation Resistance of Soil Azotobacter". Journal of Bacteriology. 89 (5): 1280-1285. ...
"Azorhizophilus paspali Taxon Passport - StrainInfo". www.straininfo.net.[dead link] "Azorhizophilus paspali (Azotobacter ...
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, Anabaena, and Clostridium) , symbiotic (ex. Rhizobium and Trichodesmium) and associative symbiotic (ex. ... "Production of nitrogen fixing Azotobacter (SR-4) and phosphorus solubilizing Aspergillus niger and their evaluation on ...
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 ... "Azotobacter vinelandii: a Pseudomonas in disguise?". Microbiology. 150 (Pt 5): 1117-9. doi:10.1099/mic.0.27096-0. PMID 15133068 ...
I. Polynucleotide phosphorylase of Azotobacter vinelandii". Biochimica et Biophysica Acta. 20 (1): 269-85. doi:10.1016/0006- ...
In Azotobacter the energy released by transferring one electron from NADH to Q is used to simultaneously boost the transfer of ... Homologous ferredoxins from Azotobacter vinelandii (Av2FeFdI; P82802) and Aquifex aeolicus (AaFd; O66511) have been ... Gao-Sheridan HS, Pershad HR, Armstrong FA, Burgess BK (March 1998). "Discovery of a novel ferredoxin from Azotobacter ... August 2017). "The Electron Bifurcating FixABCX Protein Complex from Azotobacter vinelandii: Generation of Low-Potential ...
In bacteria (for instance, Azotobacter sp.), encystment occurs by changes in the cell wall; the cytoplasm contracts and the ...
Eady RR (July 1988). "The vanadium-containing nitrogenase of Azotobacter". BioFactors. 1 (2): 111-6. PMID 3076437. Chan MK, ... such as vanadium in the nitrogenase of the nitrogen-fixing bacteria of the genus Azotobacter, tungsten in the aldehyde ...
Young, J. M.; Park, D. -C. (2007). "Probable synonymy of the nitrogen-fixing genus Azotobacter and the genus Pseudomonas". ... Rediers, H; Vanderleyden, J; De Mot, R (2004). "Azotobacter vinelandii: a Pseudomonas in disguise?". Microbiology. 150 (Pt 5): ... In the gammaproteobacterial order Pseudomonadales, the genus Azotobacter and the species Azomonas macrocytogenes are actually ...
doi:10.2138/rmg.2005.59.4. Huyer M, Page WJ (1988). "Zn2+ Increases Siderophore Production in Azotobacter vinelandii". Applied ...
Goldschmidt, Millicent C.; Wyss, Orville (January 1966). "Chelation Effects on Azotobacter Cells and Cysts". Journal of ...
Davidson IW, Lawson CJ, Sutherland IW (January 1977). "An alginate lysate from Azotobacter vinelandii phage". Journal of ...
Stevens A, Hilmoe RJ (1960). "Studies on a nuclease from Azotobacter agilis. I. Isolation and mode of action". Journal of ... doi:10.1016/S0021-9258(18)64581-8. Stevens A, Hilmoe RJ (1960). "Studies on a nuclease from Azotobacter agilis. II. Hydrolysis ...
An example of free-living bacteria is Azotobacter. Symbiotic nitrogen-fixing bacteria such as Rhizobium usually live in the ...
The NhaH family consists of proteins from Gram-negative bacteria (e.g., Leptospira, Azotobacter, Neisseria, Ralstonia, ...
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 ...
In dry soils, Azotobacter can survive in the form of cysts for up to 24 years. Representatives of the genus Azotobacter are ... "Azotobacter.org". Archived from the original (A project to study the genome of Azotobacter vinelandii) on 20 May 2013. ... nigricans and Azotobacter nigricans subsp. achromogenes; in the same year, Thompson and Skerman described Azotobacter ... "Azotobacter". Euzéby, J. P. "Azotobacter Beijerinck 1901". List of Prokaryotic names with Standing in Nomenclature. " ...
Timeline for Species Azotobacter vinelandii [TaxId:354] from c.46.1.2 Sulfurtransferase: *Species Azotobacter vinelandii [TaxId ... Species Azotobacter vinelandii [TaxId:354] from c.46.1.2 Sulfurtransferase appears in SCOP 1.61. *Species Azotobacter ... Lineage for Species: Azotobacter vinelandii. *Root: SCOP 1.63 *. Class c: Alpha and beta proteins (a/b) [51349] (117 folds). ... PDB entries in Species: Azotobacter vinelandii:. *Domain(s) for 1e0c: *. Domain d1e0ca1: 1e0c A:1-135 [32717]. ...
... Journal of Environmental Science ... Enrichment of Biogas Slurry Vermicompost with Azotobacter chroococcum and Bacillus megaterium table, th, td { border: 0px solid ... The present study has been conducted on the enrichment of biogas slurry vermicompost with microbial inoculants Azotobacter ...
Azotobacter vinelandii DJ). Find diseases associated with this biological target and compounds tested against it in bioassay ...
Azotobacter sp. DVD-7 *Azotobacter sp. DVD-8 *Azotobacter sp. FA8 *Azotobacter sp. GVT-10 *Azotobacter sp. GVT-6 *Azotobacter ... Azotobacter sp. NP11 *Azotobacter sp. NP23 *Azotobacter sp. P6-14 *Azotobacter sp. P7-20 *Azotobacter sp. P8-14 *Azotobacter sp ... Azotobacter sp. C5CO *Azotobacter sp. C5E *Azotobacter sp. CCT *Azotobacter sp. CM114 *Azotobacter sp. CM118 *Azotobacter sp. ... Azotobacter sp. Ab-HT14.2 *Azotobacter sp. AR *Azotobacter sp. ART001 *Azotobacter sp. Az15 *Azotobacter sp. Az208 *Azotobacter ...
The Gram-negative bacterium Azotobacter chroococcum NCIMB 8003 employs a new glycoside hydrolase family 70 4,6-α- ... The Gram-negative bacterium Azotobacter chroococcum NCIMB 8003 employs a new glycoside hydrolase family 70 4,6-α- ...
Azotobacter) - Pack of 2 Capsules Siesto Greens from KISANeSTORE, Indias first Agro E Store. ... Sonkul Sun Bio Azo - Azotobacter 200 grams Bio Fertilizer Nitrogen Fixing Bacteria Azotobacter&n..... ... Azoto (Azotobacter) - Pack of 2 Capsules. Description:. Azoto-CAPS are capsules containing a free-living nitrogen-fixing ... Azotobacter is used as a biofertilizer for all non-leguminous plants especially rice, cotton, vegetables, etc... It contains ...
Allows to visualize regulon content in the context of metabolic pathways ...
... Author. MAHMOUD SAZ; EL SAWY M; EL SAFTY MM. AIN SHAMS UNIV. FAC. AGRIC. AGRIC. ... MICROFLORE SOL EGYPTE AZOTOBACTER ECOLOGIE FIXATION AZOTE SOL SALIN SOL ALCALIN MICROBIOLOGIE Keyword (en). MICROFLORA EGYPT ... AZOTOBACTER ECOLOGY NITROGEN FIXATION SALINE SOIL ALKALINE SOIL MICROBIOLOGY Keyword (es). MICROBIOLOGIA Classification. Pascal ... "OCCURRENCE OF AZOTOBACTER IN SOILS OF EGYPT;s:9:\u0000*\u0000jtitle;s:0:;s:9:\u0000*\u0000stitle;s:0:;s:7:\ ...
This work cannot be reproduced in whole or in part without the express written permission of the CABRI consortium. ...
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Be the first to review "IPL Premium Azotoplus (Azotobacter) 1 kg" Cancel reply. You must be logged in to post a review. ... Chemical composition: Azotobacter. Dosage: Seed Treatment-Take Premium Azotoplus 8-10 g per kg of seed. ...
Azotobacter vinelandii DJ). Find diseases associated with this biological target and compounds tested against it in bioassay ...
Bioinformatic searches confirmed the capacity for vibrioferrin production in Azotobacter spp. and other bacteria spanning ... of the agriculturally important and widely studied model organism Azotobacter vinelandii. Using a new high-resolution liquid ...
... between dissolved natural organic matter and adsorbed DNA and their effect on natural transformation of Azotobacter vinelandii ... between dissolved natural organic matter and adsorbed DNA and their effect on natural transformation of Azotobacter vinelandii ...
... Author. * Silva, Adriana ... Entre os microrganismos produtores de PHAs, a bactéria Azotobacter vinelandii pode acumular grandes quantidades de PHB ... Substratos alternativos para a produção de poli-hidroxibutirato e alginato por Azotobacter vinelandii. 2012. 102 f. Tese ( ... Among the microorganisms producing PHAs, the bacterium Azotobacter vinelandii can accumulate large amounts of intracellular PHB ...
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Azotobacter vinelandii, a closed relative of Pseudomonas aeruginosa , has been a model for cellular differentiation in Gram- ... The Azotobacter vinelandii AlgU Regulon During Vegetative Growth and Encysting Conditions: A Proteomic Approach *Sangita ...
Many of the PGPR are fluorescent pseudomonads (Pseudomonas fluorescens), but other bacteria (Bacillus sp., Azotobacter sp., ...
P77817 (FTSZ_AZOVI) Azotobacter vinelandii. Cell division protein FtsZ UniProtKBInterProInteractive Modelling. 394 aa; Sequence ...
Degradation of Phenolic Acids by Azotobacter Species Isolated from Sorghum Fields Description: Sorghum plants excrete phenolic ... The amount of phenolic acids in soil samples were obtained by gas chromatography measurements, while Azotobacter populations ...
Azotobacter vinelandii 4xiy_c C1DFH7 99.70 3.60E-21 2.20E-25 163.20 0 0 0 0 0 0 0 0 ...
Azotobacter vinelandii DJ. Mutation(s): 0 Gene Names: mosB, Avin_43210. UniProt. ...
The growth of the Na+-dependent soil bacterium Azotobacter salinestris strain 184 was inhibited only 36% by 50 μm-carbonyl ... Examination of the role of Na+ in the physiology of the Na+-dependent soil bacterium Azotobacter salinestris * William J. Page1 ... Shivprasad S., Page W. J. 1989; Catechol formation and melanization by Na+-dependent Azotobacter chroococcum: a protective ... Page W. J., Jackson L., Shivprasad S. 1988; Sodium-dependent Azotobacter chroococcum strains are aeroadaptive, microaerophilic ...
Azotobacter sp., Rhizobium sp., IAA, Fertilizer, Arachis hypogaea..  Author Biography S. KULANDAIVEL, Thiagarajar college of ... The Indole â€" 3 â€" acetic acid (IAA) production was found to be mazimum as 1.86 ug/ml and 1.29ug/ml by Azotobacter sp. and ... AND AZOTOBACTER SP. ON INDOLE ACETIC ACID (IAA) PRODUCTION AND INDUCING VEGETATIVE CHARACTERISTICS OF ARACHIS HYPOGAEA Authors ... and Azotobacter sp. (mutants) produced only decreased shoot length, root length and number of nodules formed in Arachis ...
Cash on delivery option available purchase AZOTO - an eco friendly bio fertilizer containing azotobacter species which is free ... an eco friendly bio fertilizer containing azotobacter species which is free living nitrogen fixing bacteria Bio Fertilizer ... Azoto is an eco friendly bio fertilizer containing azotobacter species which is free living nitrogen fixing bacteria & fixes ... AZOTO - an eco friendly bio fertilizer containing azotobacter species which is free living nitrogen fixing bacteria. SIESTO ...
The density of Azotobacter in root-free soils and in the rhizosphere of several plants in arid and semi-arid Libyan regions.. ... Keywords: The density of Azotobacter in root-free soils and in the rhizosphere of several plants in arid and semi-arid Libyan ...
In Azotobacter vinelandii, deletion of the fdxA gene that encodes a well characterized seven-iron ferredoxin (FdI) is known to ... In Azotobacter vinelandii, deletion of the fdxA gene that encodes a well characterized seven-iron ferredoxin (FdI) is known to ... In Azotobacter vinelandii, the E1 subunit of the pyruvate dehydrogenase complex binds fpr promoter region DNA and ferredoxin I. ... In Azotobacter vinelandii, the E1 subunit of the pyruvate dehydrogenase complex binds fpr promoter region DNA and ferredoxin I ...
  • Entre os microrganismos produtores de PHAs, a bactéria Azotobacter vinelandii pode acumular grandes quantidades de PHB intracelular com a vantagem de utilizar durante seu crescimento uma ampla variedade de açúcares como os encontrados em melaço de cana-de-açúcar, beterraba e xarope de milho, além de resíduos da suinocultura, agroindustriais, etc. (unesp.br)
  • Among the microorganisms producing PHAs, the bacterium Azotobacter vinelandii can accumulate large amounts of intracellular PHB with the advantage that they grow a wide sugars variety like those found in molasses cane sugar, beet sugar and corn syrup, and swine waste, agribusiness, etc. (unesp.br)
  • Aerobic, inactive forms of Azotobacter vinelandii hydrogenase: activation kinetics and insensitivity to C2H2 inhibition. (ncsu.edu)
  • Azotobacter vinelandii hydrogenase (EC class 1.12), either purified or membrane-associated, was obtained aerobically in an inactive state. (ncsu.edu)
  • Azotobacter vinelandii, a closed relative of Pseudomonas aeruginosa , has been a model for cellular differentiation in Gram-negative bacteria since it forms desiccation-resistant cysts. (sciety.org)
  • In Azotobacter vinelandii, the E1 subunit of the pyruvate dehydrogenase complex binds fpr promoter region DNA and ferredoxin I. (hal.science)
  • In Azotobacter vinelandii, deletion of the fdxA gene that encodes a well characterized seven-iron ferredoxin (FdI) is known to lead to overexpression of the FdI redox partner, NADPH:ferredoxin reductase (FPR). (hal.science)
  • In Azotobacter vinelandii, the E1 subunit of the pyruvate dehydrogenase complex binds fpr promoter region DNA and ferredoxin I.. Proceedings of the National Academy of Sciences of the United States of America , 1999, pp.12389-93. (hal.science)
  • Evidence that MgATP accelerates primary electron transfer in a Clostridium pasteurianum Fe protein- Azotobacter vinelandii MoFe protein nitrogenase tight complex. (degruyter.com)
  • The enzyme from Azotobacter vinelandii is a flavoprotein (FAD). (expasy.org)
  • The first representative of the genus, Azotobacter chroococcum, was discovered and described in 1901 by Dutch microbiologist and botanist Martinus Beijerinck. (wikipedia.org)
  • The present study has been conducted on the enrichment of biogas slurry vermicompost with microbial inoculants Azotobacter chroococcum and Bacillus megaterium, optimization of inoculum level and time inoculation during vermicomposting along with the survival rate of each microbial inoculant, the total microbial population and their correlation during the storage. (scialert.net)
  • Azoto-CAPS are capsules containing a free-living nitrogen-fixing bacterium known as Azotobacter. (kisanestore.com)
  • The growth of the Na + -dependent soil bacterium Azotobacter salinestris strain 184 was inhibited only 36% by 50 μ m -carbonyl cyanide m -chlorophenylhydrazone (CCCP) at alkaline pH, whereas other species of this genus were inhibited 80-90% under the same conditions. (microbiologyresearch.org)
  • Azotobacter is a genus of usually motile, oval or spherical bacteria that form thick-walled cysts (and also has hard crust) and may produce large quantities of capsular slime. (wikipedia.org)
  • Azotobacter species are Gram-negative bacteria found in neutral and alkaline soils, in water, and in association with some plants. (wikipedia.org)
  • Cells of the genus Azotobacter are relatively large for bacteria (2-4 μm in diameter). (wikipedia.org)
  • Azoto is an eco friendly bio fertilizer containing azotobacter species which is free living nitrogen fixing bacteria & fixes free atmospheric nitrogen into available form for non legume crops. (badikheti.com)
  • To investigate the effect of different levels of nitrogen fertilizer and biofertilizer Azotobacter sp. (researchgate.net)
  • Azotobacter is used as a biofertilizer for all non-leguminous plants especially rice, cotton, vegetables, etc. (kisanestore.com)
  • however, whereas usual vegetative cells are reproductive, the cyst of Azotobacter does not serve this purpose and is necessary for surviving adverse environmental factors. (wikipedia.org)
  • The Indole â€" 3 â€" acetic acid (IAA) production was found to be mazimum as 1.86 ug/ml and 1.29ug/ml by Azotobacter sp. (innovareacademics.in)
  • It may be concluded that Soil +Vermicompost (2:1) + GA3 200 ppm + Azotobacter (0.5ml) was found best for highest survivability percentage and enhanced root parameters followed by Soil + Leaf mould (2:1) + GA3 200 ppm + Azotobacter (0.5ml). (chemistryjournals.net)
  • The present investigation entitled "Effect of different growing media, Azotobacter and GA3 on growth and survivability of transplanted air layers in Guava ( Psidium guajava L.) C.V. Gwalior- 27" was conducted at Experimental block, College of Agriculture, R.V.S.K.V.V., and Gwalior (M.P.) during the year 2020-2021. (chemistryjournals.net)
  • The density of Azotobacter in root-free soils and in the rhizosphere of several plants in arid and semi-arid Libyan regions. (lml.com.ly)
  • I have one suggestion: mention the difference among the microorganisms, for example Azotobacter, Bradyrhizobium and Rhizobium in nitrogen fixation part.I remember it is part of the homework. (kenyon.edu)
  • nov., a novel species isolated from oak in the United Kingdom, and phylogenetic considerations of the genera Pseudomonas, Azotobacter and Azomonas. (harper-adams.ac.uk)
  • When the three Azotobacter antisera were used, all Azotobacter species had mean immunological distances of less than 0.5, whereas the Azomonas species were immunologically more distant, showing that the six species of Azotobacter form an immunologically related group which is distinct from the Azomonas species. (microbiologyresearch.org)
  • Our results with the three Azomonas antisera show that each species of Azomonas is immunologically distant from the other species, as well as from the Azotobacter species. (microbiologyresearch.org)
  • Among the many species of Azotobacter, A. Crococom predominates in arable soil and is found in artificial media (2-15 mg of nitrogen established / gram carbon source). (vantikatech.com)
  • Preliminary study of taxonomy of Azotobacter and Azomonas by using rocket line immunoelectrophoresis. (microbiologyresearch.org)
  • Effects of (Azotobacter and Azosprillium) Inoculants and Chemical Fertilizers on Growth and Productivity of Canola (Brassica napus L. (scialert.net)
  • however, whereas usual vegetative cells are reproductive, the cyst of Azotobacter does not serve this purpose and is necessary for surviving adverse environmental factors. (wikipedia.org)
  • The application of inoculation with Azotobacter and Azosprillium helped to increase the yield by 21.17% over the control, raised the number of pods per plant (16.05%), number of branches (11.78%), weight of 1000 grain (2.92%) and the oil content of seeds (1.73%) but decreased (-0.24%) the number of seeds per pod. (scialert.net)