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In Vivo Oxo Transfer: Reactions of Native and W‐Substituted Dimethyl Sulfoxide Reductase Monitored by 1 H NMR Spectroscopy
Author(s) -
Stewart Lisa J.,
Bailey Susan,
Collison David,
Morris Gareth A.,
Preece Ian,
Garner C. David
Publication year - 2001
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/1439-7633(20010903)2:9<703::aid-cbic703>3.0.co;2-v
Subject(s) - dimethyl sulfoxide , trimethylamine , rhodobacter , chemistry , catalysis , flavin group , nuclear magnetic resonance spectroscopy , reductase , sulfoxide , proton nmr , stereochemistry , enzyme , photochemistry , organic chemistry , biochemistry , mutant , gene
The first direct comparison of the rate of catalysis in vivo, at corresponding Mo and W centers of an enzyme, has been achieved for the DMSO reductase of Rhodobacter capsulatus (see diagrammatic representation of the catalytic cycle). 1 H NMR spectra recorded for intact R. capsulatus cells have demonstrated that W‐DMSOR is physiologically active, but turns over at a slower rate than the native enzyme, Mo‐DMSOR. (DMSO=dimethyl sulfoxide, TMAO=trimethylamine‐N‐oxide, TMA=trimethylamine, DorC=a pentaheme c type cytochrome.