A bacterial protein from Pseudomonas, Bordetella, or Alcaligenes which operates as an electron transfer unit associated with the cytochrome chain. The protein has a molecular weight of approximately 16,000, contains a single copper atom, is intensively blue, and has a fluorescence emission band centered at 308nm.
A species of gram-negative, aerobic, rod-shaped bacteria commonly isolated from clinical specimens (wound, burn, and urinary tract infections). It is also found widely distributed in soil and water. P. aeruginosa is a major agent of nosocomial infection.
A genus of gram-negative, aerobic, motile bacteria that occur in water and soil. Some are common inhabitants of the intestinal tract of vertebrates. These bacteria occasionally cause opportunistic infections in humans.
A heavy metal trace element with the atomic symbol Cu, atomic number 29, and atomic weight 63.55.
A copper-containing plant protein that is a fundamental link in the electron transport chain of green plants during the photosynthetic conversion of light energy by photophosphorylation into the potential energy of chemical bonds.
Proteins that have one or more tightly bound metal ions forming part of their structure. (Dorland, 28th ed)
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 group of enzymes that oxidize diverse nitrogenous substances to yield nitrite. (Enzyme Nomenclature, 1992) EC 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).
Nitrate reduction process generally mediated by anaerobic bacteria by which nitrogen available to plants is converted to a gaseous form and lost from the soil or water column. It is a part of the nitrogen cycle.
Works containing information articles on subjects in every field of knowledge, usually arranged in alphabetical order, or a similar work limited to a special field or subject. (From The ALA Glossary of Library and Information Science, 1983)
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.
A rigorously mathematical analysis of energy relationships (heat, work, temperature, and equilibrium). It describes systems whose states are determined by thermal parameters, such as temperature, in addition to mechanical and electromagnetic parameters. (From Hawley's Condensed Chemical Dictionary, 12th ed)
Infections with bacteria of the genus PSEUDOMONAS.
A genus of gram-negative, aerobic, rod-shaped bacteria widely distributed in nature. Some species are pathogenic for humans, animals, and plants.
A change in electrical resistance of the skin, occurring in emotion and in certain other conditions.
The study, control, and application of the conduction of ELECTRICITY through gases or vacuum, or through semiconducting or conducting materials. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
A purely physical condition which exists within any material because of strain or deformation by external forces or by non-uniform thermal expansion; expressed quantitatively in units of force per unit area.
The physical state of supporting an applied load. This often refers to the weight-bearing bones or joints that support the body's weight, especially those in the spine, hip, knee, and foot.
The affective response to an actual current external danger which subsides with the elimination of the threatening condition.
Cortical vigilance or readiness of tone, presumed to be in response to sensory stimulation via the reticular activating system.
An essential amino acid that is necessary for normal growth in infants and for NITROGEN balance in adults. It is a precursor of INDOLE ALKALOIDS in plants. It is a precursor of SEROTONIN (hence its use as an antidepressant and sleep aid). It can be a precursor to NIACIN, albeit inefficiently, in mammals.
The accumulation of an electric charge on a object
Highly reactive molecules with an unsatisfied electron valence pair. Free radicals are produced in both normal and pathological processes. They are proven or suspected agents of tissue damage in a wide variety of circumstances including radiation, damage from environment chemicals, and aging. Natural and pharmacological prevention of free radical damage is being actively investigated.
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)
The study of chemical changes resulting from electrical action and electrical activity resulting from chemical changes.
A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
Neutral or negatively charged ligands bonded to metal cations or neutral atoms. The number of ligand atoms to which the metal center is directly bonded is the metal cation's coordination number, and this number is always greater than the regular valence or oxidation number of the metal. A coordination complex can be negative, neutral, or positively charged.
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 salt produced by the reaction of zinc oxide with acetic acid and used as an astringent, styptic, and emetic.
A species of gram-negative, aerobic bacteria isolated from soil and water as well as clinical specimens. Occasionally it is an opportunistic pathogen.
The formation of crystalline substances from solutions or melts. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)

Site-directed mutagenesis of a possible type 1 copper ligand of bilirubin oxidase; a Met467Gln mutant shows stellacyanin-like properties. (1/282)

In our previous paper, we reported a mutant of recombinant Myrothecium verrucaria bilirubin oxidase, in which the Met467 residue was replaced by Gly [Shimizu, A. et al. (1999) Biochemistry 38, 3034-3042]. This mutant displayed a remarkable reduction in enzymatic activity and an evident decrease in the intensity of the absorption band around 600 nm (type 1 charge transfer transition). In this study, we report the preparation of three Met467 mutants (Met467Gln, Met467His, and Met467Arg) and characterize their enzymatic activities, midpoint potentials, and absorption and ESR spectra. Met467His and Met467Arg show no enzymatic activity and a great reduction in the intensity of the absorption band around 600 nm. Furthermore, their ESR spectra show no type 1 copper signal, but only a type 2 copper signal; however, oxidation by ferricyanide caused the type 1 copper signal to appear. On the other hand, Met467Gln as expressed shows both type 1 and type 2 copper signals in its ESR spectrum, the type 1 copper atom parameters being very different from usual blue copper proteins but very similar to those of stellacyanin. The enzymatic activity of the Met467Gln mutant for bilirubin is quite low (0.3%), but the activity for potassium ferrocyanide is similar (130%) to that of the wild type enzyme. These results indicate that Met467 is important for characterizing the features of the type 1 copper of bilirubin oxidase.  (+info)

Pseudoazurin mediates periplasmic electron flow in a mutant strain of Paracoccus denitrificans lacking cytochrome c550. (2/282)

A periplasmic protein able to transfer electrons from cytoplasmic membrane to the periplasmic nitrite reductase (cytochrome cd1) has been purified from the anoxically grown cytochrome c550 mutant strain Pd2121 and shown to be pseudoazurin by several independent criteria (molecular mass, copper content, visible spectrum, N-terminal amino acid sequence). Under our assay conditions, the half-saturation of electron transport occurred at about 10 microM pseudoazurin; the reaction was retarded by increasing ionic strength.  (+info)

Crystal structure determinations of oxidized and reduced pseudoazurins from Achromobacter cycloclastes. Concerted movement of copper site in redox forms with the rearrangement of hydrogen bond at a remote histidine. (3/282)

The crystal structures of oxidized and reduced pseudoazurins from a denitrifying bacterium, Achromobacter cycloclastes IAM1013, have been determined at 1.35- and 1.6-A resolutions, respectively. The copper site in the oxidized state exhibits a distorted tetrahedral structure like those of other pseudoazurins. However, not only a small change of the copper geometry, but concerted peptide bond flips are identified. The imidazole ring of remote His6 has a hydrogen bonding distance of 2.73 A between N-delta1(His6) and O-gamma1(Thr36) in the oxidized protein. When the protein is reduced at pH 6.0, the imidazole ring rotates by 30.3 degrees and moves 1.00 A away from the position of the oxidized state. A new hydrogen bond between N-epsilon2(His6) and O-epsilon1(Glu4) is formed with a distance of 3.03 A, while the hydrogen bond between N-delta1(His6)-O-gamma1(Thr36) is maintained with an interatomic distance of 2.81 A. A concomitant peptide bond flip of main chain between Ile34 and Thr36 occurs.  (+info)

A spectroscopic and calorimetric investigation on the thermal stability of the Cys3Ala/Cys26Ala azurin mutant. (4/282)

The disulfide bond connecting Cys-3 and Cys-26 in wild type azurin has been removed to study the contribution of the -SS- bond to the high thermal resistance previously registered for this protein (. J. Phys. Chem. 99:14864-14870). Site-directed mutagenesis was used to replace both cysteines for alanines. The characterization of the Cys-3Ala/Cys-26Ala azurin mutant has been carried out by means of electron paramagnetic resonance spectroscopy at 77 K, UV-VIS optical absorption, fluorescence emission and circular dichroism at room temperature. The results show that the spectral features of the Cys-3Ala/Cys-26Ala azurin resemble those of the wild type azurin, indicating that the double mutation does not affect either the formation of the protein's overall structure or the assembly of the metal-binding site. The thermal unfolding of the Cys-3Ala/Cys-26Ala azurin has been followed by differential scanning calorimetry, optical absorption variation at lambda(max) = 625 nm, and fluorescence emission using 295 nm as excitation wavelength. The analysis of the data shows that the thermal transition from the native to the denaturated state of the modified azurin follows the same multistep unfolding pathway as observed in wild type azurin. However, the removal of the disulfide bridge results in a dramatic reduction of the thermodynamic stability of the protein. In fact, the transition temperatures registered by the different techniques are down-shifted by about 20 degrees C with respect to wild type azurin. Moreover, the Gibbs free energy value is about half of that found for the native azurin. These results suggest that the disulfide bridge is a structural element that significantly contributes to the high stability of wild type azurin.  (+info)

Photoinduced electron transfer in singly labeled thiouredopyrenetrisulfonate azurin derivatives. (5/282)

A novel method for the initiation of intramolecular electron transfer reactions in azurin is reported. The method is based on laser photoexcitation of covalently attached thiouredopyrenetrisulfonate (TUPS), the reaction that generates the low potential triplet state of the dye with high quantum efficiency. TUPS derivatives of azurin, singly labeled at specific lysine residues, were prepared and purified to homogeneity by ion exchange HPLC. Transient absorption spectroscopy was used to directly monitor the rates of the electron transfer reaction from the photoexcited triplet state of TUPS to Cu(II) and the back reaction from Cu(I) to the oxidized dye. For all singly labeled derivatives, the rate constants of copper ion reduction were one or two orders of magnitude larger than for its reoxidation, consistent with the larger thermodynamic driving force for the former process. Using 3-D coordinates of the crystal structure of Pseudomonas aeruginosa azurin and molecular structure calculation of the TUPS modified proteins, electron transfer pathways were calculated. Analysis of the results revealed a good correlation between separation distance from donor to Cu ligating atom (His-N or Cys-S) and the observed rate constants of Cu(II) reduction.  (+info)

The effect of pressure and guanidine hydrochloride on azurins mutated in the hydrophobic core. (6/282)

The unfolding of the blue-copper protein azurin from Pseudomonas aeruginosa by guanidine hydrochloride, under nonreducing conditions, has been studied by fluorescence techniques and circular dichroism. The denaturation transition may be fitted by a simple two-state model. The total free energy change from the native to the unfolded state was 9.4 +/- 0.4 kcal.mol-1, while a lower value (6.4 +/- 0.4 kcal.mol-1) was obtained for the metal depleted enzyme (apo-azurin) suggesting that the copper atom plays an important stabilization role. Azurin and apo-azurin were practically unaffected by hydrostatic pressure up to 3000 bar. Site-directed mutagenesis has been used to destabilize the hydrophobic core of azurin. In particular either hydrophobic residue Ile7 or Phe110 has been substituted with a serine. The free energy change of unfolding by guanidinium hydrochloride, resulted to be 5.8 +/- 0.3 kcal.mol-1 and 4.8 +/- 0.3 kcal.mol-1 for Ile7Ser and Phe110Ser, respectively, showing that both mutants are much less stable than the wild-type protein. The mutated apoproteins could be reversible denatured even by high pressure, as demonstrated by steady-state fluorescence measurements. The change in volume associated to the pressure-induced unfolding was estimated to be -24 mL.mol-1 for Ile7Ser and -55 mL.mol-1 for Phe110Ser. These results show that the tight packing of the hydrophobic residues that characterize the inner structure of azurin is fundamental for the protein stability. This suggests that the proper assembly of the hydrophobic core is one of the earliest and most crucial event in the folding process, bearing important implication for de novo design of proteins.  (+info)

Gated and ungated electron transfer reactions from aromatic amine dehydrogenase to azurin. (7/282)

Interprotein electron transfer (ET) occurs between the tryptophan tryptophylquinone (TTQ) prosthetic group of aromatic amine dehydrogenase (AADH) and copper of azurin. The ET reactions from two chemically distinct reduced forms of TTQ were studied: an O-quinol form that was generated by reduction by dithionite, and an N-quinol form that was generated by reduction by substrate. It was previously shown that on reduction by substrate, an amino group displaces a carbonyl oxygen on TTQ, and that this significantly alters the rate of its oxidation by azurin (Hyun, Y-L., and Davidson V. L. (1995) Biochemistry 34, 12249-12254). To determine the basis for this change in reactivity, comparative kinetic and thermodynamic analyses of the ET reactions from the O-quinol and N-quinol forms of TTQ in AADH to the copper of azurin were performed. The reaction of the O-quinol exhibited values of electronic coupling (H(AB)) of 0.13 cm(-1) and reorganizational energy (lambda) of 1.6 eV, and predicted an ET distance of approximately 15 A. These results are consistent with the ET event being the rate-determining step for the redox reaction. Analysis of the reaction of the N-quinol by Marcus theory yielded an H(AB) which exceeded the nonadiabatic limit and predicted a negative ET distance. These results are diagnostic of a gated ET reaction. Solvent deuterium kinetic isotope effects of 1.5 and 3.2 were obtained, respectively, for the ET reactions from O-quinol and N-quinol AADH indicating that transfer of an exchangeable proton was involved in the rate-limiting reaction step which gates ET from the N-quinol, but not the O-quinol. These results are compared with those for the ET reactions from another TTQ enzyme, methylamine dehydrogenase, to amicyanin. The mechanism by which the ET reaction of the N-quinol is gated is also related to mechanisms of other gated interprotein ET reactions.  (+info)

Localization of periplasmic redox proteins of Alcaligenes faecalis by a modified general method for fractionating gram-negative bacteria. (8/282)

A lysozyme-osmotic shock method is described for fractionation of Alcaligenes faecalis which uses glucose to adjust osmotic strength and multiple osmotic shocks. During phenylethylamine-dependent growth, aromatic amine dehydrogenase, azurin, and a single cytochrome c were localized in the periplasm. Their induction patterns are different from those for the related quinoprotein methylamine dehydrogenase and its associated redox proteins.  (+info)

Understanding how the folding of proteins establishes their functional characteristics at the molecular level challenges both theorists and experimentalists. The simplest test beds for confronting this issue are provided by electron transfer proteins. The environment provided by the folded protein to the cofactor tunes the metals electron transport capabilities as envisioned in the entatic hypothesis. To see how the entatic state is achieved one must study how the folding landscape affects and in turn is affected by the metal. Here, we develop a coarse-grained functional to explicitly model how the coordination of the metal (which results in a so-called entatic or rack-induced state) modifies the folding of the metallated Pseudomonas aeruginosa azurin. Our free-energy functional-based approach directly yields the proper nonlinear extra-thermodynamic free energy relationships for the kinetics of folding the wild type and several point-mutated variants of the metallated protein. The results agree ...
Dive into the research topics of Molecular monolayers and interfacial electron transfer of Pseudomonas aeruginosa azurin on Au(111). Together they form a unique fingerprint. ...
The triplet metal-to-ligand charge transfer (^3MLCT) dynamics of two structurally characterized Re^I(CO)_3(phen)(HisX)-modified (phen = 1,10-phenanthroline; X = 83, 109) Pseudomonas aeruginosa azurins have been investigated by picosecond time-resolved infrared (TRIR) spectroscopy in aqueous (D_2O) solution. The ^3MLCT relaxation dynamics exhibited by the two Re^I−azurins are very different from those of the sensitizer [Re^I(CO)_3(phen)(im)]+ (im = imidazole). Whereas the Re^I(CO)_3 intramolecular vibrational relaxation in Re^I(CO)_3(phen)(HisX)Az (4 ps) is similar to that of [ReI(CO)3(phen)(im)]+ (2 ps), the medium relaxation is much slower (∼250 vs 9.5 ps); the 250-ps relaxation is attributable to reorientation of D_2O molecules as well as structural reorganization of the rhenium chromophore and nearby polar amino acids in each of the modified proteins. ...
Azurin is a bacterial blue copper protein found in Pseudomonas, Bordetella, or Alcaligenes bacteria, which undergoes oxidation-reduction between Cu(I) and Cu(II), and transfers single electrons between enzymes associated with the cytochrome chain. The protein has a molecular weight of approximately 16,000, contains a single copper atom, is intensively blue, and has a fluorescence emission band centered at 308 nm. Azurins and pseudoazurins participate in denitrification processes in bacteria. Azurin and cytochrome c551 are involved in electron transfer during denitrification in P. aeruginosa. Azurin from P aeruginosa is a type I blue copper protein with a molecular mass of 14 kDa, while cytochrome c551 (9 kDa) is a haem-containing cytochrome. Azurin possesses a relatively large hydrophobic patch close to the active site, and two residues in this hydrophobic patch, Met-44 and Met-64, are believed to be involved in its interaction with the redox partners cytochrome c551 and nitrite reductase ...
The coordination chemistry and electron-transfer properties of a single-site mutant of the mononuclear copper electron-transfer protein azurin from Pseudomonas aeruginosa have been studied. The active-site cysteine at position 112 was replaced by an aspartate (Cys112Asp) to assess directly the importance of this ligand to the structure-function properties of azurin. Although the mutant protein retains a high-affinity copper-binding active site, the absorption and EPR spectra of Cu[superscript II]Cys112Asp azurin are quite distinct from those of the wild-type protein and indicate the presence of a normal (type 2) copper center. A Cu[superscript II/I] reduction potential of 180 mV vs. NHE (pH 7.0) was obtained through a redox titration experiment with cytochrome c[subscript 551]. The Co[superscript II] derivative of Cys112Asp azurin was prepared and found to be amenable to paramagnetic NMR spectroscopy. In conjunction with electronic absorption data, the NMR data were used to generate a computer ...
filtered_set; syntelog; UniRef90: B6UB13_MAIZE Blue copper protein n=1 (Zea mays) Exp=7e-60; maizesequence.org: RefSeq_peptide:NP_001152236; blue copper protein , UniGene:Zm.136022; Blue copper protein , UniGene:Zm.24862; Blue copper protein , Uniprot/SPTREMBL:B6TFN3; Blue copper protein , Uniprot/SPTREMBL:B6UB13; Blue copper protein , RefSeq_peptide:NP_001149576; blue copper protein , RefSeq_dna:NM_001158764; blue copper protein (LOC100285874) mRNA , RefSeq_dna:NM_001156104; blue copper protein (LOC100283202) mRNA , GO:0009055; electron carrier activity , GO:0005507; copper ion binding , EntrezGene:100285874; blue copper protein , EntrezGene:100283202; blue copper ...
The bacterial redox protein azurin has been shown to be able to enter into cancer cells and induce apoptosis by stabilizing p53. Although the formation of a complex between the two proteins has been demonstrated, little is known about their binding ...
The present invention relates to compositions comprising CpG rich DNA from Pseudomonas aeruginosa. The compositions optionally comprise a cupredoxin. The present invention includes specific CpG DNAs from Pseudomonas aeruginosa that are useful for treating cancer and other conditions in patients. These compositions are optionally in a pharmaceutically acceptable carrier and also optionally comprise a cupredoxin. The present invention further relates to methods to express proteins near cancer cells. These methods may be used to express therapeutic or diagnostic proteins near cancer cells in a patient suffering from cancer or other conditions, and can also be used for diagnosing cancer in a patient. This method uses the gene for azurin from P. aeruginosa as an expression system for azurin or heterologous proteins in P. aeruginosa or heterologous cells.
Sabale S. S.*, Koli A.D., Marathe R. J. and Phatake Y. B.. ABSTRACT. The secondary metabolites from microorganisms play a vital role in developing new chemotherapeutics. Microorganisms especially bacteria produce different secondary metabolites which had proved to be one of the most important source of lead compounds. In the present study potent azurin producing bacteria were isolated and screen from from three soil samples (Maharashtra, India) and identified by morphological, biochemical and molecular method (16s r DNA) as Pseudomonas aeruginosa which produce a biologically active protein azurin, that has array of bioactivities. The produced azurin was extracted and qualitatively characterized by using conventional and modern analytical methods. The spectroscopic study shows lambda max of produced protein as 225nm. Finally the production process of azurin was optimized by classical method. The selected strain of bacteria produces maximum azurin in selective media-I containing yeast extract and ...
Tyrosine and tryptophan play critical roles in facilitating proton-coupled electron transfer (PCET) processes essential to life. The local protein environment is anticipated to modulate the thermodynamics of amino acid radicals to achieve controlled, unidirectional PCET. Herein, square-wave voltammetry was employed to investigate the electrostatic effects on the redox properties of tryptophan in two variants of the protein azurin. Each variant contains a single redox-active tryptophan, W48 or W108, in a unique and buried protein environment. These tryptophan residues exhibit reversible square-wave voltammograms. A Pourbaix plot, representing the reduction potentials versus pH, is presented for the non-H-bonded W48, which has potentials comparable to those of tryptophan in solution. The reduction potentials of W108 are seen to be increased by more than 100 mV across the same pH range. Molecular dynamics shows that, despite its buried indole ring, the N-H of W108 hydrogen bonds with a water ...
Mono- and Stereopictres of 5.0 Angstrom coordination sphere of Copper atom in PDB 2oj1: Disulfide-Linked Dimer of Azurin N42C/M64E Double Mutant
Azurin (Az) has been considered as the research hotspot in molecular electronics, as well as a promising material for building functional devices on the molecular scale because of its special electrical properties and force-dependent conductance effects. Here we carry out an in-depth investigation combined w
The copper-sulphur bond which binds cysteinate to the metal centre is a key factor in the spectroscopy of blue copper proteins. We present theoretical calculations describing the electronically excited states of small molecules, including CuSH, CuSCH_3, (CH_3)_2SCuSH, (imidazole)-CuSH and (imidazole)_2-CuSH, derived from the active site of blue copper proteins that contain the copper-sulphur bond in order to identify small molecular systems that have electronic structure that is analogous to the active site of the proteins. Both neutral and cationic forms are studied, since these represent the reduced and oxidised forms of the protein, respectively. For CuSH and CuSH^+, excitation energies from time-dependent density functional theory with the B97-1 exchange-correlation functional agree well with the available experimental data and multireference configuration interaction calculations. For the positive ions, the singly occupied molecular orbital is formed from an antibonding combination of a 3d ...
This site is solely for the enjoyment of FREE Live music from recordings of independent origin (ROIO), which have not been officially released. There is no money make from this site, and no donations will be accepted. This id dedicate just to the music.. This site does not host any files. It is only linking to independent sites 3rd party sites offering downloads. If youre an artist (or a legal representative of an artist or its estate) and you dont want your ROIOs linked for free among your fans, you may opt out any time by sending e-mail to the site admin. We will then put you in our list of not allowed artists.. This will halt all sharing of your ROIOs via 3rd part links within a few minutes.. The contact form is below. BTW, the ROIOs exist, you cant make them vanish. So, why not let your fans get them for free from one another instead of having to purchase them from commercial bootleggers on auction sites?. ...
In a BIM for a mononuclear centre, the central atom (metal) is written first, followed by the endogenous ligands (amino acid residues), and then the exogenous ligands, e.g. water. If the ligating atom needs to be indicated to avoid ambiguity, the symbol for this is separated from the ligand symbol by a dot, e.g. NE.His stands for the Nε atom of a His residue. This is a simplistic description that does not take into account the stereochemistry at the metal atom. The polyhedral symbol is not mandatory for it may be unknown. It also does not make sense for polynuclear metal centres (see below).. Example 4.1 in Table 4 shows a mononuclear centre found in the blue copper protein azurin. In this centre, one copper atom is coordinated by the Nδ atoms of two His residues, one mainchain oxygen derived from Gly, one Sδ atom of a Met residue and one Sγ atom of a Cys residue. The coordination geometry is trigonal bipyramidal (TBPY-5; the polyhedral symbols used are as in Table S3 in Additional file ...
TY - JOUR. T1 - Azurin-like protein blocks invasion of Toxoplasma gondii through potential interactions with parasite surface antigen SAG1. AU - Naguleswaran, Arunasalam. AU - Fialho, Arsenio M.. AU - Chaudhari, Anita. AU - Chang, Soo Hong. AU - Chakrabarty, Ananda M.. AU - Sullivan, William. PY - 2008/2. Y1 - 2008/2. N2 - Some pathogenic bacteria produce factors that have evolved a capacity to neutralize competing microbes. The cupredoxin family protein azurin, produced by Pseudomonas aeruginosa, exhibits a remarkable ability to impede invasion of a number of diverse intracellular pathogens, including the human AIDS virus human immunodeficiency virus type 1 and the protozoan parasite Plasmodium falciparum (which causes malaria). Here we report that azurin and an azurin-like protein (Laz) from gonococci/meningococci have activity against Toxoplasma, an apicomplexan parasite that causes opportunistic infection in immunocompromised individuals. We demonstrate that the mechanism of action for Laz ...
1GY1: Crystal Structures of the met148Leu and Ser86Asp Mutants of Rusticyanin from Thiobacillus Ferrooxidans: Insights Into the Structural Relationship with the Cupredoxins and the Multi Copper Proteins
We have studied long-range electron transfer through various lengths of helical peptides from 8 mer (24 Å) up to 80 mer (120 Å) in self-assembled monolayers prepared on a gold surface. Helical peptides carrying a redox-active ferrocene unit and a disulfide group at the respective terminals were synthesized and immobilized on gold via a gold-sulfur linkage to form a well-defined monolayer with vertical helix orientation, and the electron transfer from the ferrocene unit to gold through the helical peptides was studied by electrochemistry. The electron transfer showed a very shallow distance dependence and high activation energies, both of which are characteristic of a hopping mechanism. Detailed theoretical calculations successfully demonstrated that a hopping mechanism with the amide groups as hopping sites is responsible for the long-range electron transfer, which enables ultralong-range electron transfer over 120 Å with the 80 mer helical peptide.
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Osmotics Blue Copper 5 Firming Elasticity Repair 1 oz -Osmotics Blue Copper 5 Firming Elasticity RepairDescription: Osmotics Blue Copper 5 Firming Ela
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Structures of Pseudomonas putida azurin in two polymorphs, one crystallized in the presence and one in the absence of zinc acetate, have been determined at 1.60 and 1.92 Å resolution, respectively. The protein forms nearly identical dimers in both asymmetric units which differ in relative monomer orientation from dimers of other known azurins; chelation of one of the zinc ions by a twofold-related pair of molecules explains the observed change in lattice parameters upon zinc incorporation ...
RN [1] RM PMID:21749987 RT S-bacillithiolation protects against hypochlorite stress in Bacillus subtilis as revealed by transcriptomics and redox proteomics. RA Chi BK, Gronau K, Mader U, Hessling B, Becher D, Antelmann H RL Mol Cell Proteomics. 2011 Nov;10(11):M111.009506. doi: 10.1074/mcp.M111.009506. RN [2] RM PMID:20712413 RT Bacillithiol, a new player in bacterial redox homeostasis. RA Helmann JD RL Antioxid Redox Signal. 2011 Jul 1;15(1):123-33. doi: 10.1089/ars.2010.3562. RN [3] RM PMID:22938038 RT S-bacillithiolation protects conserved and essential proteins against hypochlorite stress in firmicutes bacteria. RA Chi BK, Roberts AA, Huyen TT, Basell K, Becher D, Albrecht D, Hamilton CJ, Antelmann H RL Antioxid Redox Signal. 2013 Apr 10;18(11):1273-95. doi: 10.1089/ars.2012.4686 ...
1CUR: NMR solution structure of Cu(I) rusticyanin from Thiobacillus ferrooxidans: structural basis for the extreme acid stability and redox potential.
InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
Our innovative use of cell penetrating peptides derived from microbial and plant proteins is without precedent in cancer treatment. CDG has broadly filed U.S. and foreign patents covering use of cupredoxin family of proteins and their fragments. The patent portfolio also includes numerous international patent applications on CDGs core technology and improvements.. Our patents include composition of matter including modifications thereof, utility claims as a single or multiple-agent therapy; therapeutic adjunct; and for diagnostic uses. The portfolio includes indications for cancer as well as allied and infectious diseases. We continue to file new utility and provisional patent applications as our research advances.. Cytoxic Factors for Modulating Cell Death. [7084105, 7491394, 7888468]. Cupredoxin Derived Transport Agents and Methods of Use Thereof. [7691383, 8206685, 8530635]. Transport Agents for Crossing the Blood-brain barrier and into Brain Cancer Cells, and Methods of Use ...
A handsome, large deciduous tree, with elegant spreading branches and dark purple leaves which turn copper in autumn and a shimmering bronze in spring.
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such a new brilliant approach to eradicate cancer! this is interesting and beneficial as the bacterial proteins termed azurin & ATP-01 not only found effective in anticancer but also cancer preventive activity. Besides, because those bacteria are naturally-occurring human bacterial symbionts, i think it is higher chances to reduce/prevent immunogenicity and always non-toxic to human. its great to hear that ATP-01 also effective in anti-HIV/AIDS activity, should be a great invention and discovery! ...
I am from Brazil and we are a very passionate people and especially in Sao Paulo, where I live, sex its like breathing. Recently something happened that change my lifestyle. The problem was that my husband started suffering from impotency. Disturbing our entire relationship slowly but surely we started distancing ourselves each day, leaving much of our needs unfulfilled. My marriage was saved in a day when I was browsing the internet looking for online pharmacies, and I found www.worldselectshop.com. Youre high quality herbal products restored my husbands vitality and love for me. Thank you www.worldselectshop.com for saving our sex life.. Merced Azurin ...
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A catalytically active tryptophan radical has been demonstrated to be involved in the long-range electron transfer to the heme cofactor of lignin peroxidase (LiP) from Phanerochaete chrysosporium although no direct detection by EPR spectroscopy of the tryptophan radical intermediate has been reported to date. An engineering-based approach has been used to manipulate the microenvironment of the redox-active tryptophan site in LiP and Coprinus cinereus Peroxidase (CiP), allowing the direct evidence of the tryptophan radical species. In light of the newly available EPR experimental data, we performed a quantum mechanical/molecular mechanics computational study to characterize the tryptophan radicals in the above protein matrices as well as in pristine LiP. The nature of the tryptophan radicals is discussed together with the analysis of their environment with the aim of understanding the different behavior of pristine LiP in comparison with that of LiP and CiP variants ...
|jats:p|The pseudoazurin gene from Thiosphaera pantotropha has been cloned and sequenced. The deduced amino acid sequence showed that the protein contains an unusually alanine-rich signal peptide, 22 amino acid residues in length, which targets the protein to the periplasm. This pseudoazurin was expressed in large amounts in the periplasm of Escherichia coli when the gene with its native ribosome-binding site was placed downstream of the lac promoter. Removal of a putative hairpin-forming structure upstream of the ribosome-binding site increased the yield of the purified protein to ∼80 mg/l. The recombinant protein is indistinguishable from that purified from its natural host. A primer extension study indicated that the pseudoazurin structural gene (pazS) is under the control of the Fnr/Nnr regulatory system, but no promoter-binding sequence could be recognized. The amino acid sequence of pseudoazurin from Paracoccus denitrificans is also reported.|/jats:p|
Blue copper binding proteins are prevalent in all forms of life, yet most of them have not been functionally identified. These proteins have special folding characteristics, which allow them to bind a single copper atom, a co-factor responsible for their unique redox characteristics. Because copper is a transition metal with a 3d configuration, it can accept or give a single electron, changing its oxidation state from +2 (3d,sup,9,/sup,) to +1 (3d,sup,10,/sup,). This property makes blue copper proteins excellent candidates for electron transfer in biological systems. This report focuses on two closely related blue copper proteins - chemocyanin from Lilium longiflorum and plantacyanin from Arabidopsis thaliana . These proteins have been classified as blue copper proteins, primarily based on the sequence features commonly found in the amino acid sequences of the other members in this family. However, they have neither been purified nor characterized biochemically. On the other hand, it has been ...
1l9s: Directing the mode of nitrite binding to a copper-containing nitrite reductase from Alcaligenes faecalis S-6: characterization of an active site isoleucine.
TY - JOUR. T1 - Numerical solution of solvent reorganization energy and its application in electron transfer reaction. AU - Bi, Ting Jun. AU - Ming, Mei Jun. AU - Ren, Hai Sheng. AU - Ma, Jian Yi. AU - Li, Xiang Yuan. PY - 2014/8/27. Y1 - 2014/8/27. N2 - According to our recent studies on the nonequilibrium solvation, the solvent reorganization energy λs is found to be the cost of maintaining the residual polarization, which equilibrates with the constraining extra electric field. In this work, a matrix form of λs has been formulated based our new analytical expression of the solvent reorganization energy. By means of the integral equation formulation-polarizable continuum model (IEF-PCM), a new numerical algorithm for λs has been implemented as a subroutine coupled with the Q-Chem package. Then, we have performed a comparison of numerical results with analytical solution obtained by two-sphere model for λs in self-exchange electron transfer (ET) reaction of He-He+ system. The numerical ...
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The Crystal Blue Copper Sulfate in granular form is the only way to go. The product appears to be expensive but in the big picture it is required to completely eradicate the algae. Its the only product we will use if and when the algae reappears. Note: Dyeing the pond is very important also. We strongly recommend the use of Prime Source WSB .... ...
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Sigma-Aldrich offers abstracts and full-text articles by [Yasuko Manabe, Mayumi Takagi, Mio Nakamura-Yamada, Naoko Goto-Inoue, Masato Taoka, Toshiaki Isobe, Nobuharu L Fujii].
Planchestainer, Matteo and Segaud, Nathalie and Shanmugam, Muralidharan and McMaster, Jonathan and Paradisi, Francesca and Albrecht, Martin (2018) Carbene in cupredoxin protein scaffolds: replacement of a histidine ligand in the active site substantially alters copper redox properties. Angewandte Chemie International Edition, 57 (33). pp. 10677-10682. ISSN 1521-3773 Carucci, Cristina and Bruen, Larah and Gascón, Victoria and Paradisi, Francesca and Magner, Edmond (2018) Significant enhancement of structural stability of the hyperhalophilic ADH from Haloferax volcanii via entrapment on metal organic framework support. Langmuir . ISSN 0743-7463 Contente, Martina L. and Paradisi, Francesca (2018) Self-sustaining closed-loop multienzyme mediated conversion of amines into alcohols in continuous reactions. Nature Catalysis . ISSN 2520-1158 Cassidy, Jennifer and Paradisi, Francesca (2018) Haloquadratum walsbyi yields a versatile, NAD+/NADP+ dual affinity, thermostable, alcohol dehydrogenase (HwADH). ...
This bacterial enzyme contains a flavin (FAD) subunit and a cytochrome c subunit. -!- The flavin subunit abstracts two hydrogen atoms from the substrate, forming a quinone methide intermediate, then hydrates the latter at the benzylic carbon with a hydroxyl group derived from water. -!- The protons are lost to the bulk solvent, while the electrons are passed to the heme on the cytochrome subunit, and from there to azurin, a small copper-binding protein that is co-localized with the enzyme in the periplasm. -!- The first hydroxylation forms 4-hydroxybenzyl alcohol; a second hydroxylation converts this into 4-hydroxybenzaldehyde. -!- Formerly EC 1.17.99.1 ...
TY - JOUR. T1 - Design of functional metalloproteins. AU - Lu, Yi. AU - Yeung, Natasha. AU - Sieracki, Nathan. AU - Marshall, Nicholas M.. PY - 2009/8/13. Y1 - 2009/8/13. N2 - Metalloproteins catalyse some of the most complex and important processes in nature, such as photosynthesis and water oxidation. An ultimate test of our knowledge of how metalloproteins work is to design new metalloproteins. Doing so not only can reveal hidden structural features that may be missing from studies of native metalloproteins and their variants, but also can result in new metalloenzymes for biotechnological and pharmaceutical applications. Although it is much more challenging to design metalloproteins than non-metalloproteins, much progress has been made in this area, particularly in functional design, owing to recent advances in areas such as computational and structural biology.. AB - Metalloproteins catalyse some of the most complex and important processes in nature, such as photosynthesis and water ...
Motivation: With the advent of genome sequencing, a huge database of protein primary sequences has been accumulating. In parallel, a number of tools to investigate and expand upon this information, e.g. reconstructing and building relationships between protein families and superfamilies, have been developed. Metalloproteins are proteins capable of binding one or more metal ions, which are required for their biological function or for regulation of their activities or for structural purposes. Sometimes, metal binding can be observed in vitro but not be physiologically relevant. At present, there is a lack of specific tools to address the matter of the identification of metalloproteins in databases of gene sequences. Results: In the present work, an approach exploiting metal-binding patterns (MBPs) of metalloproteins present in the Protein Data Bank to search gene banks for new metalloproteins is presented and applied to copper proteins. Nearly 100 different MBPs have been identified and then used ...
Our previous AM1 semiempirical molecular orbital studies on the electron self-exchange reaction between -diaminobenzene (PPD) and its radical cation have been extended to include dynamics calculations of the inner-sphere vibrational frequency, , and a configuration interaction (Cl) study of the distance dependence
Fox, Lucius Seiberling (1989) Intramolecular electron transfer in an iridium d [supercript 8]-d [superscript 8] donor-acceptor system. Dissertation (Ph.D.), California Institute of Technology. http://resolver.caltech.edu/CaltechETD:etd-06072007-081509 Karas, Jennifer Lynn (1989) Long-range electron transfer in ruthenium-labelled myoglobin. Dissertation (Ph.D.), California Institute of Technology. http://resolver.caltech.edu/CaltechETD:etd-06082007-092426 Kormann, Claudius (1989) Synthesis and characterization of quantum size metal oxide colloidal particles. Photocatalytic peroxide formation on ZnO and TiO2. Dissertation (Ph.D.), California Institute of Technology. http://resolver.caltech.edu/CaltechETD:etd-05182007-110357 Selman, Mary (1989) Preparation and characterization of an intramolecular electron transfer in a pentaammineruthenium derivative of Candida krisei cytochrome c. Dissertation (Ph.D.), California Institute of Technology. ...
Professor Armstrong leads a research group concerned with mechanistic and exploratory Bioinorganic Chemistry. The principal aims are to understand the chemical reactions carried out by the active sites of metalloproteins (a well-known example would be the Fe-porphyrin group as occurs in haemoglobin) and to elucidate how long-range electron transfer in complex protein systems is coupled to catalysis and ion/proton transfer.. Subjects range from the properties of unstable Fe-S clusters and Fe(IV)=O (to most chemists an unusual oxidation state) to medically important respiratory chain electron transport enzymes such as succinate dehydrogenase. To study these systems, his group uses a range of kinetic techniques, and is currently developing a powerful new method in which the chemistry of metalloprotein active sites is probed electrochemically while they are absorbed on a carbon electrode surface ...
It is generally assumed that tethering enhances rates of electron harvesting and delivery to active sites in multidomain enzymes by proximity and sampling mechanisms. Here, we explore this idea in a tethered 3-domain, trimeric copper-containing nitrite reductase. By reverse engineering, we find that …
Copper sulfate crystals are the easiest and brightest blue crystals that you can grow. Here's how you can grow copper sulfate crystals yourself.
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The invention relates to novel methods and compositions for the detection of analytes using the nuclear reorganization energy, λ, of an electron transfer process.
Four azurin molecules bind each p53 monomer with high affinity. The p53/azurin complex travels to the nucleus, where p53 ... Azurin is a small, periplasmic, bacterial blue copper protein found in Pseudomonas, Bordetella, or Alcaligenes bacteria. Azurin ... Although this pathway plays a significant role in azurins anticancer activity, the details of the interaction between azurin ... making azurin is a useful model system for studying long-range, intraprotein electron transfer (LRET). Azurin is a tetrameric ...
... and oxidised azurin, whereas its 3 products are arsenate, reduced azurin, and hydrogen ion. This enzyme belongs to the family ... Arsenate reductase (azurin) (EC 1.20.9.1) is an enzyme that catalyzes the chemical reaction arsenite + H2O + 2 azurinox ⇌ {\ ... The systematic name of this enzyme class is arsenite:azurin oxidoreductase. This enzyme is also called arsenite oxidase. The ...
Azurin. A, B. 128. Pseudomonas aeruginosa PAO1. Mutation(s): 2 Gene Names: azu, PA4922. ... M121E Azurin.. Liu, J., Meier, K.K., Tian, S., Zhang, J.L., Guo, H., Schulz, C.E., Robinson, H., Nilges, M.J., Munck, E., Lu, Y ... Herein we report spectroscopic and X-ray crystallographic studies of Fe(II)-M121E azurin (Az), by replacing the axial Met121 ... Herein we report spectroscopic and X-ray crystallographic studies of Fe(II)-M121E azurin (Az), by replacing the axial Met121 ...
AZURIN. A, B. 128. Pseudomonas aeruginosa. Mutation(s): 0 Find proteins for P00282 (Pseudomonas aeruginosa (strain ATCC 15692 ... Pseudomonas aeruginosa Azurin Re(phen)(CO)3(His83). *DOI: 10.2210/pdb1JZI/pdb ...
A PHS activity assay was adapted to investigate the activities of PHM-Azurin and NiR-Azurin using an already 2 e- reduced ... To study this reaction, an azurin protein scaffold model was used. Our models contain the naturally occurring T1 copper center ... 2014). Phenoxazinone synthase Activity of Azurin Variants. Retrieved from the University of Minnesota Digital Conservancy, http ...
Copper uptake by folded apo-azurin, to govern active (holo) protein, is slow (tau approximately 14 min, 50:1 copper-to-protein ... To uncover the role of one cofactor, we have examined the folding kinetics of Pseudomonas aeruginosa azurin, a small blue- ... Copper removal produces apo-azurin which adopts a folded structure identical to that of the holo-form. The folding and ... Copper binding before polypeptide folding speeds up formation of active (holo) Pseudomonas aeruginosa azurin.. Pozdnyakova I1, ...
Establishing the entatic state in folding metallated Pseudomonas aeruginosa azurin. Proceedings of the National Academy of ... modifies the folding of the metallated Pseudomonas aeruginosa azurin. Our free-energy functional-based approach directly yields ... level of detail to explicitly model how the geometric entatic state of the metal modifies the dynamic folding nucleus of azurin ...
Azurin (Az) has been considered as the research hotspot in molecular electronics, as well as a promising material for building ... Azurin (Az) has been considered as the research hotspot in molecular electronics, as well as a promising material for building ... The dynamic conductance response and mechanics-modulated memristive behavior of the Azurin monolayer under cyclic loads ... The dynamic conductance response and mechanics-modulated memristive behavior of the Azurin monolayer under cyclic loads X. ...
Azurin was detected in the CM of transfected MSC and, upon treatment with hazu-MSC-CM, we observed a decrease in cancer cell ... Azurin was detected in the CM of transfected MSC and, upon treatment with hazu-MSC-CM, we observed a decrease in cancer cell ... Moreover, expression of azurin caused no changes in MSC expression profile of cytokines relevant in the context of cancer ... Moreover, expression of azurin caused no changes in MSC expression profile of cytokines relevant in the context of cancer ...
wt) azurin and zinc-reconstituted wt azurin were labeled on the The kinetics of ET are strikingly similar between protein- N ... wt azurin) or 1-octanethiol (zinc azurin and N42C). For of the SAM thickness. At large distances, the non-adiabatic more ... N42C azurin was prepared similarly (see section 10 in the ET within productive protein ET complexes occurs in the Supporting ... described by van Baarle et al.[45] Azurin was immobilized on the The rate of electron transfer between an ET protein and a ...
In this study, azurin gene ( azu) from a native Pseudomonas aeruginosastrain... ... Azurin is a novel anticancer protein, mainly produced from Pseudomonas aeruginosa and few other Gram-negative bacteria. ... The azurin gene (418 bp) was sequenced and submitted in Genbank. The PCR amplicon was digested with BamHI and HindIII and ... In this study, azurin gene (azu) from a native Pseudomonas aeruginosa strain SSj was amplified using PCR with specific primers ...
The genes encoding Pseudomonas aeruginosa azurin variants W48 (Y72F/Y108F), W48F (W48F/Y72F/Y108F), and W108 (W48F/Y72F/Y108W) ... Impact of Local Electrostatics on the Redox Properties of Tryptophan Radicals in Azurin: Implications for Redox-Active ... employed to investigate the electrostatic effects on the redox properties of tryptophan in two variants of the protein azurin. ... employed to investigate the electrostatic effects on the redox properties of tryptophan in two variants of the protein azurin. ...
The 2.4-Å resolution X-ray crystal structure of Cu[superscript II] Cys112Asp azurin is reported and confirms this ligand set ... Ni[superscript II]-substituted Cys112Asp azurin was also made, but unlike Cu[superscript II] and Co[superscript II], the Ni[ ... Mizoguchi, Tadashi Jack (1996) Probing the role of the active-site Cysteine of Azurin by site-directed mutagenesis. ... The electronic spectroscopy of Ni[superscript II] Cys112Asp azurin suggests the existence of some bonding interaction with the ...
... ... In the p53-null UISO-Mel-6 cells, azurin is localized only in the cytosol. Thus, intracellular trafficking of azurin to the ... Kankersoorten , Huidkankers , Azurin, een eiwit gehaald uit bacterien zorgt voor… , 18 maart 20112: Over Azurin, een bacterieel ... However, this is the first report that azurin is also effective as an anticancer agent.. Azurin was isolated from the growth ...
DESIGN AND ENGINEERING OF I) AMINO ACID SCHIFF BASE COMPLEXES AND II) CUPREDOXIN AZURIN AND CUA AZURIN. ... CUPREDOXIN AZURIN AND CUA AZURIN. [email protected] Repository. ... interest is to tune the redox potential of cupredoxin T1 azurin ...
This graph shows the total number of publications written about "Azurin" by people in this website by year, and whether "Azurin ... "Azurin" is a descriptor in the National Library of Medicines controlled vocabulary thesaurus, MeSH (Medical Subject Headings) ... Below are the most recent publications written about "Azurin" by people in Profiles. ...
6 to be accurate for single-step tunneling in azurin.. Interestingly, the values of R coh and τcoh in azurin are not very ... Correlation Functions in Azurin. To our knowledge, the only computation of the short-time decay of CFC (t) for a biological ET ... 8 for azurin with an average τcoh ≃ 30 fsec, λ ≃ 1 eV, and Δ E 0 ≃ -λ, gives a correction of 0.8% of the Marcus rate. As in the ... We compute the autocorrelation function of the donor-acceptor tunneling matrix element 〈TDA (t)TDA (0)〉 for six Ru-azurin ...
In this study, azurin presence was Azurin is a potent anticancer protein which has the ability to interfere in tumor growth. ... Presence of azurin gene was confirmed by PCR, and partially purified azurin protein was detected by SDS-PAGE according to ... The purpose of this study was to isolate azurin producing native Pseudomonas spp along with the confirmation of azurin presence ... The purpose of this study was to isolate azurin producing native Pseudomonas isolates along with the confirmation of azurin ...
Recombinant Bordetella bronchiseptica Azurin(BB3856) von Cusabio bei SZABO-SCANDIC erhältlich. Weiteres zu Proteine & Peptide ...
Uploaded by Miriam Azurin. Related Interests. *Food Security. *Subsidy. *Foods. *World Trade Organization ...
by Azurin, J. C Material type: Book; Format: print Publisher: Makati : J. C. Azurin Foundation, 1988Availability: Items ... Disease surveillance in primary health care : proceedings of the 10th SEAMIC Seminar / edited by J. C. Azurin.. by (10th: ... Primary health care in national development : proceedings of the 8th SEAMIC Workshop / editor, J. C. Azurin.. by (8th: SEAMIC ... Primary health care : innovations in the Philippine health system , 1981-1985 / J. C. Azurin.. ...
CRYSTAL STRUCTURE OF THE DISULPHIDE BOND-DEFICIENT AZURIN MUTANT C3A/C26A: HOW IMPORTANT IS THE S-S BOND FOR FOLDING AND ... Bonander, N. et al., Crystal structure of the disulfide bond-deficient azurin mutant C3A/C26A: how important is the S-S bond ... CRYSTAL STRUCTURE OF THE DISULPHIDE BOND-DEFICIENT AZURIN MUTANT C3A/C26A: HOW IMPORTANT IS THE S-S BOND FOR FOLDING AND ...
STRUCTURE OF APO-AZURIN FROM ALCALIGENES DENITRIFICANS AT 1.8 ANGSTROMS RESOLUTION ... STRUCTURE OF APO-AZURIN FROM ALCALIGENES DENITRIFICANS AT 1.8 ANGSTROMS RESOLUTION. Coordinates. PDB Format Method. X-RAY ... Shepard, W.E. et al., Structure of apo-azurin from Alcaligenes denitrificans at 1.8 A resolution. Acta Crystallogr.,Sect.D ( ...
Azurin is a bacterial protein produced by Pseudomonas aeruginosa with known anticancer properties. A peptide fragment of Azurin ... Azurin (P28) fusion protein mediated photodynamic therapy in the treatment of malignant tumors. ... Nour El Din, Suzanne (2017): Azurin (P28) fusion protein mediated photodynamic therapy in the treatment of malignant tumors. ...
Azurin, Azurin: chemistry, circular dichroism, Circular Dichroism: methods, copper, Copper: chemistry, CRYSTALLOGRAPHY, LIGANDS ... derivative of Pseudomonas aeruginosa azurin (NiAz). Our analysis of these spectra confirms that the electronic ground state of ...
The binding sites of Copper atom in the structure of Azurin Dimer, Crosslinked Via Disulfide Bridge (pdb code 1jvo). This ... Copper in the structure of Azurin Dimer, Crosslinked Via Disulfide Bridge (pdb 1jvo). ...
Structures of Pseudomonas putida azurin in two polymorphs, one crystallized in the presence and one in the absence of zinc ...
AZURIN; 23 I&N Dec. 695 (BIA 2005). ID 3505 (PDF). An alien who, prior to the 1996 amendments made to former section 212(c) of ...
The Bacterial Protein Azurin Enhances Sensitivity of Oral Squamous Carcinoma Cells to Anticancer Drugs By Jeong-Hae Choi, Moo- ... Internalization of bacterial redox protein azurin * Less cytotoxicity to combination therapy of 5-fluorouracil and cisplatin ...

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