Document Detail

Structural basis for nitrous oxide generation by bacterial nitric oxide reductases.
MedLine Citation:
PMID:  22451105     Owner:  NLM     Status:  MEDLINE    
The crystal structure of the bacterial nitric oxide reductase (cNOR) from Pseudomonas aeruginosa is reported. Its overall structure is similar to those of the main subunit of aerobic and micro-aerobic cytochrome oxidases (COXs), in agreement with the hypothesis that all these enzymes are members of the haem-copper oxidase superfamily. However, substantial structural differences between cNOR and COX are observed in the catalytic centre and the delivery pathway of the catalytic protons, which should be reflected in functional differences between these respiratory enzymes. On the basis of the cNOR structure, we propose a possible reaction mechanism of nitric oxide reduction to nitrous oxide as a working hypothesis.
Yoshitsugu Shiro; Hiroshi Sugimoto; Takehiko Tosha; Shingo Nagano; Tomoya Hino
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Philosophical transactions of the Royal Society of London. Series B, Biological sciences     Volume:  367     ISSN:  1471-2970     ISO Abbreviation:  Philos. Trans. R. Soc. Lond., B, Biol. Sci.     Publication Date:  2012 May 
Date Detail:
Created Date:  2012-03-27     Completed Date:  2012-10-16     Revised Date:  2013-06-26    
Medline Journal Info:
Nlm Unique ID:  7503623     Medline TA:  Philos Trans R Soc Lond B Biol Sci     Country:  England    
Other Details:
Languages:  eng     Pagination:  1195-203     Citation Subset:  IM    
RIKEN SPring-8 Center, Sayo, Hyogo, Japan.
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MeSH Terms
Crystallography, X-Ray
Models, Molecular
Nitric Oxide / metabolism*
Nitrous Oxide / metabolism*
Oxidoreductases / chemistry,  metabolism*
Pseudomonas aeruginosa / enzymology,  metabolism*
Reg. No./Substance:
10024-97-2/Nitrous Oxide; 10102-43-9/Nitric Oxide; EC 1.-/Oxidoreductases; EC reductase

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