Authors: KuanI Chen Alastair G McEwan Paul V Bernhardt
Publish Date: 2010/10/27
Volume: 16, Issue: 2, Pages: 227-234
Abstract
The bacterial molybdoenzyme dimethyl sulfoxide DMSO reductase from Rhodobacter capsulatus catalyzes the reduction of DMSO to dimethyl sulfide in anaerobic respiration In its native state DMSO reductase is reduced to its active state by a pentaheme cytochrome DorC Alternatively we show that DMSO reductase catalysis may be driven electrochemically using a series of homologous coordination compounds as mediating synthetic electron donors All mediators are macrocyclic hexaaminecobaltII complexes in their active form differing principally in their redox potentials over a range of about 250 mV Thus each complex presents a different reductive driving force to DMSO reductase and this leads to pronounced differences in the electrocatalytic behavior as measured by cyclic voltammetry Digital simulation of the experimental voltammetry enables the critical features of the catalytic cycle to be extracted
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