- 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...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1021/bi002452u
-
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- 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
- Copyright date:
- 2001
Journal article
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.
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