The quinoprotein methanol dehydrogenase (MDH) contains a Ca2+ ion at the active site. Ca(2-)-free enzyme (from a processing mutant) was used to obtain enzyme containing Sr2+ or Ba2+, the Ba(2+)-MDH being the first enzyme to be described in which a Ba2+ ion functions at the active site. The activation energy for oxidation of methanol by Ba(2+)-MDH is less than half that of the reaction catalysed...

“Candidatus Methylomirabilis oxyfera” is a newly discovered anaerobic methanotroph that, surprisingly, oxidizes methane through an aerobic methane oxidation pathway. The second step in this aerobic pathway is the oxidation of methanol. In Gramnegative bacteria, the reaction is catalyzed by pyrroloquinoline quinone (PQQ)-dependent methanol dehydrogenase (MDH). The genome of “Ca. Methylomirabilis...

We recently showed that methanol emitted by wounded plants might function as a signaling molecule for plant-to-plant and plant-to-animal communications. In mammals, methanol is considered a poison because the enzyme alcohol dehydrogenase (ADH) converts methanol into toxic formaldehyde. However, the detection of methanol in the blood and exhaled air of healthy volunteers suggests that methanol m...

Methyl formate synthase, which catalyzes methyl formate formation during the growth of methylotrophic yeasts, was purified to homogeneity from methanol-grown Candida boidinii and Pichia methanolica cells. Both purified enzymes were tetrameric, with identical subunits with molecular masses of 42 to 45 kDa, containing two atoms of zinc per subunit. The enzymes catalyze NAD(+)-linked dehydrogenati...

Many methylotrophs, microorganisms that consume carbon compounds lacking carbon-carbon bonds, use two different systems to oxidize methanol for energy production and biomass accumulation. The MxaFI methanol dehydrogenase (MDH) contains calcium in its active site, while the XoxF enzyme contains a lanthanide in its active site. The genes encoding the MDH enzymes are differentially regulated by th...

The structure of methanol dehydrogenase (MDH) at 0.194 nm (1.94 A) has been used to provide a model structure for part of a membrane quinoprotein glucose dehydrogenase (GDH). The basic superbarrel structure is retained, along with the tryptophandocking motifs. The active-site regions are similar, but there are important differences, the most important being that GDH lacks the novel disulphide r...

Ethanol and fomepizole are used as antidotes for poisoning with ethylene glycol or methanol. Both ethylene glycol and methanol are metabolized by the enzyme alcohol dehydrogenase. Ethanol is a substrate for alcohol dehydrogenase and fomepizole is an inhibitor of this enzyme. This review pays attention to the differences between ethanol and fomepizole. The advantages and disadvantages of both an...