Electronic state of the dimethyl sulfoxide reductase active site.
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.
Hofmann
Matthias
M
Anorganisch-Chemisches Institut, Ruprecht-Karls-Universität Heidelberg, Im Neuenheimer Feld 270, 69120 Heidelberg, Germany. matthias.hofmann@aci.uni-heidelberg.de
D001665:Binding Sites; D004583:Electrons; D007506:Iron-Sulfur Proteins / Q000737:chemistry*; D008962:Models, Theoretical; D010088:Oxidoreductases / Q000737:chemistry*; D013816:Thermodynamics
D007506:Iron-Sulfur Proteins; D010088:Oxidoreductases; C045664:dimethyl sulfoxide reductase