Direct Electrochemistry of a Bacterial Sulfite Dehydrogenase

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Abstract
Sulfite dehydrogenase from Starkeya novella is an αβ heterodimer comprising a 40.6 kDa subunit (containing the Mo cofactor) and a smaller 8.8 kDa heme c subunit. The enzyme catalyses the oxidation of sulfite to sulfate with the natural electron acceptor being cytochrome c550. Its catalytic mechanism is thought to resemble that found in eukaryotic sulfite oxidases. Using protein film voltammetry and redox potentiometry, we have identified both Mo- and heme-centered redox responses from the enzyme immobilized on a pyrolytic graphite working electrode: Em,8 (FeIII/II) +177 mV; Em,8 (MoVI/V) +211 mV and Em,8 (MoV/IV) −118 mV vs NHE; Upon addition of sulfite to the electrochemical cell a steady-state voltammogram is observed and an apparent Michaelis constant (Km) of 26(1) μM was determined for the enzyme immobilized on the working electrode surface, which is comparable with the value obtained from solution assays.