The structure and mechanism of methanol dehydrogenase.
This is a review of recent work on methanol dehydrogenase (MDH), a pyrroloquinoline quinone (PQQ)-containing enzyme catalysing the oxidation of methanol to formaldehyde in methylotrophic bacteria. Although it is the most extensively studied of this class of dehydrogenases, it is only recently that there has been any consensus about its mechanism. This is partly due to recent structural studies on normal and mutant enzymes and partly due to more definitive work on the mechanism of related alcohol and glucose dehydrogenases. This work has also led to conclusions about the subsequent path of electrons and protons during the reoxidation of the reduced quinol form of the prosthetic group.
Anthony
Christopher
C
Division of Biochemistry and Molecular Biology, School of Biological Sciences, University of Southampton S016 7PX, Hants, Southampton, UK. C.Anthony@soton.ac.uk
Williams
Paul
P
D000429:Alcohol Oxidoreductases / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D045542:PQQ Cofactor; D015363:Quinolones / Q000737:chemistry; D011809:Quinones / Q000737:chemistry
D015363:Quinolones; D011809:Quinones; D045542:PQQ Cofactor; D000429:Alcohol Oxidoreductases; C019641:alcohol dehydrogenase (acceptor)