Mediated, anaerobic voltammetry of sulfite oxidase

Abstract

The anaerobic voltammetry of the Mo/Fe enzyme, sulfite oxidase (SO), is described for the mediators cytochrome c, [Ru(NH3)6]3+/2+, TMPD+/0, and [Co(bpy)3]3+/2+. Theory derived for steady-state voltammetric catalysis correctly predicts the observed concentration and scan-rate dependencies of the catalytic waves. The instances for which existing ECcat theories may be applied to two catalytic reactions coupled to an interfacial charge transfer are considered. The bimolecular rate constant for the reaction of [Co(bpy)3]3+ with reduced SO is calculated and determined to be approximately 5 .times. 104 .cntdot. mol-1 l .cntdot. s-1. The appearance of catalytic prepeaks at low sulfite concentrations is noted and the shape of corresponding l/t curves from chronoamperometry is examined. The analytical implications of the novel time dependence of the catalytic current under these conditions are discussed.