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Determination of an optimal potential window for catalysis by E. coli dimethyl sulfoxide reductase and hypothesis on the role of Mo(V) in the reaction pathway.

Abstract:

Protein film voltammetry (PFV) of Escherichia coli dimethyl sulfoxide (DMSO) reductase (DmsABC) adsorbed at a graphite electrode reveals that the catalytic activity of this complex Mo-pterin/Fe-S enzyme is optimized within a narrow window of electrode potential. The upper and lower limits of this window are determined from the potential dependences of catalytic activity in reducing and oxidizing directions; i.e., for reduction of DMSO (or trimethylamine-N-oxide) and oxidation of trimethylphos...

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Publication status:
Published

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Publisher copy:
10.1021/bi002452u

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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Inorganic Chemistry
Role:
Author
Journal:
Biochemistry
Volume:
40
Issue:
10
Pages:
3117-3126
Publication date:
2001-03-05
DOI:
EISSN:
1520-4995
ISSN:
0006-2960
URN:
uuid:292016da-ba3a-455d-94bb-5c322ac5f671
Source identifiers:
31844
Local pid:
pubs:31844

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