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Volume 142, Issue 11

Kinetic analysis and substrate specificity of dimethyl sulfoxide reductase Free

Abstract

We have characterized the substrate specificity of dimethyl sulfoxide reductase (DmsABC) of by determining and values for 22 different substrates. The enzyme has a very broad substrate specificity. The values varied 470-fold, while values varied only 20-fold, implicating as the major determinant of / values. Sulfoxides and pyridine -oxide exhibited the lowest values, followed by aliphatic -oxides. The values for these compounds also followed the same pattern. Substitution at the 2 or 3 position of the pyridine -oxide ring had little effect on while substitution at the 4 position had a greater effect, and increased . Negatively charged substrates were poorly accepted. A few compounds that are not - or -oxides were also reduced by the enzyme. Most compounds reduced by DmsABC were not toxic to under anaerobic growth conditions, and was able to use many of these compounds anaerobically as terminal electron acceptors in the presence of glycerol. Anaerobic growth on sulfoxides is solely due to DmsABC expression. However, there appears to be another as yet unidentified terminal reductase capable of using pyridine -oxides as terminal electron acceptors.

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Keyword(s): anaerobic reductase , molybdoenzyme , pyridine N-oxide , S- or N-oxide and trimethylamine N-oxide
©Society for General Microbiology 1996
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1996-11-01
2024-04-18
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Kinetic analysis and substrate specificity of Escherichia coli dimethyl sulfoxide reductase
Microbiology 142, 3231 (1996); https://doi.org/10.1099/13500872-142-11-3231
/content/journal/micro/10.1099/13500872-142-11-3231
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