Mediated electrochemistry of dimethyl sulfoxide reductase from Rhodobacter capsulatus.

Electrochemically driven catalysis of the bacterial enzyme dimethyl sulfoxide (DMSO) reductase (Rhodobacter capsulatus) has been studied using the macrocyclic complex (trans-6,13-dimethyl-1,4,8,11-tetraazacyclotetradecane-6,13-diamine)cobalt(III) as a mediator. In the presence of both DMSO and DMSO reductase, the normal transient Co(III/II) voltammetric response of the complex is transformed into an amplified and sigmoidal (steady-state) waveform characteristic of a catalytic EC' mechanism. At low concentrations of DMSO (approximately K (M)) or high mediator concentrations (more than the concentration of DMSO reductase), the steady-state character of the voltammetric response disappears and is replaced by more complicated waveforms that are a convolution of transient and steady-state behavior as different steps within the catalytic cycle become rate limiting. Through digital simulation of cyclic voltammetry performed under conditions where the sweep rate, DMSO concentration, DMSO reductase concentration and mediator concentration were varied systematically, we were able to model all voltammograms with a single set of rate and equilibrium constants which provide new insights into the kinetics of the DMSO reductase catalytic mechanism that have hitherto been inaccessible from steady state or stopped flow kinetic studies.