Abstract
Computations suggest that in contrast with small models the active site geometry of reduced dimethyl sulfoxide reductase might prefer a triplet over a singlet electronic state.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Binding Sites
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Electrons
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Iron-Sulfur Proteins / chemistry*
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Models, Theoretical
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Oxidoreductases / chemistry*
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Thermodynamics
Substances
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Iron-Sulfur Proteins
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Oxidoreductases
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dimethyl sulfoxide reductase