Abstract
Methanol dehydrogenase (MDH; EC 1.1.99.8) catalyses the oxidation of methanol to formaldehyde in the periplasm of methylotrophic bacteria during growth on methanol or methane. It was first described in Methylobacterium extorquens (Anthony and Zatman, 1964a,b) and has subsequently been shown to be the one feature that is common to almost all methylotrophs in which it often constitutes up to 15% of their soluble protein (see Anthony, 1986 for a review of the basic enzymology of a wide range of MDHs). MDH is a soluble quinoprotein which has pyrroloquinoline quinone (PQQ) as its prosthetic group and it uses a specific cytochrome, cytochrome cL as electron acceptor. It is usually assayed in a dye-linked system at high pH when ammonia is required as activator. It has an α2β2 structure; each α
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