The active site of methanol dehydrogenase (MDH) contains a rare disulfide bridge between adjacent cysteine residues. As a vicinal disulfide, the structure is highly strained, suggesting it might work together with the pyrroloquinoline quinone (PQQ) prosthetic group and the Ca ion in the catalytic turnover during methanol (CHOH) oxidation. We purify MDH from (Bath) with the disulfide bridge broken into two thiols.
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