Electronic state of the dimethyl sulfoxide reductase active site

Inorg Chem. 2008 Jul 7;47(13):5546-8. doi: 10.1021/ic800519d. Epub 2008 Jun 6.

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

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Electrons
  • Iron-Sulfur Proteins / chemistry*
  • Models, Theoretical
  • Oxidoreductases / chemistry*
  • Thermodynamics

Substances

  • Iron-Sulfur Proteins
  • Oxidoreductases
  • dimethyl sulfoxide reductase