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2 edition of Physico-chemical studies on Pseudomonas aeruginosa nitrite reductase. found in the catalog.

Physico-chemical studies on Pseudomonas aeruginosa nitrite reductase.

John Antony Sutherland

Physico-chemical studies on Pseudomonas aeruginosa nitrite reductase.

by John Antony Sutherland

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  • 15 Currently reading

Published by University of East Anglia in Norwich .
Written in English


Edition Notes

Thesis (Ph.D.) - University of East Anglia, School of Biological Sciences 1983.

ID Numbers
Open LibraryOL13809295M

As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from Cited by: Nitrit reduktaza (formira NO) (EC , cd-citohrom nitritna reduktaza, citohrom cO2, NO 2+ oksidoreduktaza, citohrom cd, citohrom cd1, hidroksilamin (akceptor) reduktaza, metil viologen-nitritna reduktaza, nitritna reduktaza (citohrom, formira NO)) je enzim sa sistematskim imenom nitric-oksid:fericitohrom-c oksidoreduktaza. Ovaj enzim katalizuje sledeću hemijsku BRENDA: BRENDA entry.

Azurin is a small, periplasmic, bacterial blue copper protein found in Pseudomonas, Bordetella, or Alcaligenes moderates single-electron transfer between enzymes associated with the cytochrome chain by undergoing oxidation-reduction between Cu(I) and Cu(II).Each monomer of an azurin tetramer has a molecular weight of approximately 14kDa, contains a CDD: cd   Cytochrome c nitrite reductase catalyzes the six-electron reduction of nitrite to ammonia without the release of potential reaction intermediates, such as NO or hydroxylamine. On the basis of the crystallographic observation of reaction intermediates and of density functional calculations, we present a working hypothesis for the reaction mechanism of this multiheme Cited by:

  Crude oil spills represent a major ecological threat because of the chemical inertness of the constituent n -alkanes. The Gram-negative bacterium Pseudomonas aeruginosa is one of the few bacterial species able to metabolize such compounds. Three chromosomal genes, rubB, rubA1, and rubA2 coding for an NAD(P)H:rubredoxin reductase (RdxR) and Cited by: Kim C-H and Hollocher TC () 15 N tracer studies on the reduction of nitrite by the purified dissimilatory nitrite reductase of Pseudomonas aeruginosa. J. Biol. Chem. – PubMed Google ScholarCited by: 2.


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Physico-chemical studies on Pseudomonas aeruginosa nitrite reductase by John Antony Sutherland Download PDF EPUB FB2

The biochemistry and molecular biology of nitrite reductase, a key enzyme in the dissimilatory denitrification pathway of Ps aeruginosa which reduces nitrite to NO, is reviewed in this paper.

The enzyme is a non-covalent homodimer, each subunit containing one heme c Cited by:   Cd 1 nitrite reductase catalyzes the conversion of nitrite to NO in denitrifying bacteria. Reduction of the substrate occurs at the d 1-heme site, which faces on the distal side some residues thought to be essential for substrate binding and report the results obtained by mutating to Ala the two invariant active site histidines, His and His, of the enzyme from Pseudomonas.

A nitrite reductase was purified more than fold from extracts prepared from actively denitrifying P. enzyme reduced nitrite to nitric oxide when either reduced flavins (Riboflavin H 2, FMNH 2 FADH 2) reduced pyocyanine, reduced methylene blue or reduced 1, 4-naphthoquinone was the electronTPNH and reduced cytochrome c were Cited by: QM−MM Study of Nitrite Reduction by Nitrite Reductase of Pseudomonas aeruginosa Article in The Journal of Physical Chemistry B (46) October with.

The one electron reduction of nitrite to NO, catalyzed in vivo by a group of enzymes called nitrite reductases (NIRs), has been extensively investigated due to its relevance in the processes of denitrification.

The heme containing NIRs are soluble noncovalent homodimers with two heme groups in each subunit: a d1 heme, the site of nitrite reduction, and a type c heme, Cited by: Abstract. Genetic studies on denitrifiers have been largely limited to Pseudomonas aeruginosa because of its well studied genetic systems of gene transfer—conjugative and transductional.

Studies on this organism have identified and located a number of genes encoding the enzymes that mediate nitrate reduction including the assimilatory and dissimilatory nitrate and nitrite Cited by: 1.

The nitrite reductase activity of Ps. aeruginosa NiR was investigated by performing electrochemical measurements in solutions containing cytochrome c as electron shuttle, the enzyme NiR and the substrate, nitrite, in non-limiting concentrations. Fig. 3 shows the effect of the addition of increasing amounts of NiR on the CV curve of 38 μM cytochrome c in 50 Cited by: Pseudomonas aeruginosa (PA) is considered to be bacteria with a low capability to produce nitrite.

To investigate the incidence of a positive urine nitrite test. PDF | On Aug 1,S. Hasnain and others published XAFS and crystallographic studies of an azurin and a blue copper nitrite reductase from a denitrifying bacterium |.

Bruce Ward, in Molecular Medical Microbiology (Second Edition), Nitrite Reductases. Nitrite reductases in denitrifying bacteria are of two types, either cytochrome cd 1 or copper nitrite reductases, often designated cd1NIR and CuNIR (naming analogous to NOR for nitric oxide reductase).

For example, cytochrome cd 1 is found in P. denitrificans, P. aeruginosa. Mucoid, mucA mutant Pseudomonas aeruginosa cause chronic lung infections in cystic fibrosis (CF) patients and are refractory to phagocytosis and antibiotics. Here we show that mucoid bacteria perish during anaerobic exposure to 15 mM nitrite (NO 2 –) at pHwhich mimics CF airway g required a pH lower than 7, implicating formation of nitrous Cited by:   Härtig E, Zumft WG () Kinetics of nirS expression (cytochrome cd 1 nitrite reductase) in Pseudomonas stutzeri during the transition from aerobic respiration to denitrification: evidence for a denitrification-specific nitrate- and nitrite Cited by: Abstract: Nitrite reductase (nirS) is a key enzyme of denitrification catalyzing the one electron reduction of nitrite (NO 2-) to nitrogen monoxide (NO).In this study, nirS gene was cloned from Pseudomonas aeruginosa HGP9 strain.

The phylogenetic tree was constructed and the secondary structure was predicted by bioinformatics. Results showed that nirS gene was % similar to the nitrite Author: Yongliang Zheng, Zhonghua Wu, Jianping Gan, Jianping Fang, Shiwang Liu, Deli Liu, Yuling Zhong.

The impact of biofilm formation and bacterial solutions of Desulfovibrio vulgaris (a sulfate reducing bacteria, SRB) and Pseudomonas aeruginosa (PAO1, denitrifying bacteria) on the corrosion of cast iron was assessed and compared in this study.

Corrosion experiments were separately conducted in respective culture media (in-situ) and in % NaCl (ex-situ, pH 4).Cited by: The dissimilatory nitrite reductase (cytochrome c,d1) from Pseudomonas aeruginosa was observed at pH to catalyze nitrosyl transfer (nitrosation) between [15N]nitrite and several N.

Pseudomonas aeruginosa (PA) is an important airway pathogen of cystic fibrosis and chronic obstructive disease patients. Multiply drug resistant PA is becoming increasing prevalent and new strategies are needed to combat such insidious organisms.

We have previously shown that a mucoid, mucA22 mutant PA is exquisitely sensitive to acidified nitrite (A-NO 2 −, pH ) at Cited by: 9.

A c‐type monohemic ferricytochrome c (11 kDa) was isolated from the soluble extract of a marine denitrifier, Pseudomonas nautica straingrown under anaerobic conditions with nitrate as final electron acceptor. The NH 2 ‐terminal sequence and the amino acid composition of the cytochrome were determined.

The heme iron of the cytochrome c has Cited by: Considerable lung injury results from the inflammatory response to Pseudomonas aeruginosa infections in patients with cystic fibrosis (CF).

The P. aeruginosa laboratory strain PAO1, an environmental isolate, and isolates from CF patients were cultured in vitro and outer membrane vesicles from those cultures were quantitated, purified, and by: Volumenumber 2 FEES July A copper-containing protein that inhibits nitrite reductase from Pseudomonas aeruginosa A.V.

Karapetian, M.G. Kamalian and R.M. Nalbandyan Institute of Biochemistry, Academy of Sciences, Armenian SSR, YerevanUSSR Received 26 May A non-blue copper-containing glycoprotein was isolated from Pseudomonas by: 1.

cd1 nitrite reductase (NIR) is a key enzyme in the denitrification process that reduces nitrite to nitric oxide (NO).

It contains a specialized d1-heme cofactor, found only in this class of enzymes, where the substrate, nitrite, binds and is converted to NO.

For a long time, it was believed that NO must be released from the ferric d1-heme to avoid enzyme inhibition by the formation of Cited by:. The spectroscopic and mechanistic properties of the Cu-containing active site of azurin from Pseudomonas aeruginosa were investigated by the construction of a mutant in which one of the ligands of the metal, His46, was replaced by a glycine.

Although the mutation creates a hole in the interior of the protein, the 3D structure of the protein does not change to any appreciable .Electrochemical study of the intermolecular electron transfer to Pseudomonas aeruginosa cytochrome cd 1 nitrite reductase Article in Electrochimica Acta 48(8).

(b) Structure of an iron-containing porphyrin ring from P. aeruginosa nitrite reductase (PDB entry 1n15, Nurizzo et al., ). (c) Superposition of Cu–CAII N terminus with the P. aeruginosa nitrite reductase heme with an RMSD of Å. It is important to note that the N terminus T-1 site is less ordered in comparison to the rest of the.