Document Detail


Two CO molecules can bind concomitantly at the diiron site of NO reductase from Bacillus azotoformans.
MedLine Citation:
PMID:  15563131     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
CO complexes formed in reduced nitric oxide reductase from Bacillus azotoformans were investigated with resonance Raman and FTIR techniques. These experiments shows the presence of two nu(C-O) bands, one at approximately 1970 cm-1 assigned to the heme-CO complex, and one at approximately 2070 cm-1 from the non-heme iron, FeBCO. At cryogenic temperatures, the heme-CO complex adopts a semi-bridging configuration with FeB which decreases its stretching frequency to approximately 1910 cm-1 and decreases the nu(C-O) of FeBCO by approximately 20 cm-1. The concomitant binding of two CO molecules, one per iron(II) at the active site, is consistent with the formation of a [{FeNO}7]2 iron-nitrosyl dimer during substrate turnover. This study strongly supports the notion that this family of enzymes utilizes a reaction mechanism based on catalysis by proximity, where the formation of two iron-nitrosyl groups promotes N-N bond formation.
Authors:
Shen Lu; Suharti; Simon de Vries; Pierre Moënne-Loccoz
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Journal of the American Chemical Society     Volume:  126     ISSN:  0002-7863     ISO Abbreviation:  J. Am. Chem. Soc.     Publication Date:  2004 Dec 
Date Detail:
Created Date:  2004-11-25     Completed Date:  2005-05-02     Revised Date:  2012-05-28    
Medline Journal Info:
Nlm Unique ID:  7503056     Medline TA:  J Am Chem Soc     Country:  United States    
Other Details:
Languages:  eng     Pagination:  15332-3     Citation Subset:  IM    
Affiliation:
Department of Environmental & Biomolecular Systems, OGI School of Science & Engineering, Oregon Health & Science University, Beaverton, OR 97006-8921, USA.
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MeSH Terms
Descriptor/Qualifier:
Bacillus / enzymology*
Bacterial Proteins / chemistry,  metabolism
Binding Sites
Carbon Monoxide / chemistry,  metabolism*
Chlorides / chemistry
Heme / chemistry,  metabolism*
Nonheme Iron Proteins / chemistry,  metabolism*
Oxidoreductases / chemistry,  metabolism*
Spectroscopy, Fourier Transform Infrared
Spectrum Analysis, Raman
Grant Support
ID/Acronym/Agency:
GM 18865/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/Chlorides; 0/Nonheme Iron Proteins; 14875-96-8/Heme; 630-08-0/Carbon Monoxide; EC 1.-/Oxidoreductases; EC 1.7.2.5/nitric-oxide reductase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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