The biochemistry of methanol dehydrogenase
Methanol dehydrogenase (MDH) is responsible for oxidation of methanol to formaldehyde in almost all bacteria growing aerobically on methane or methanol; it is a periplasmic quinoprotein which passes its electrons to a specific c-type cytochrome which is usually called cytochrome c L (Anthony, 1986, 1992, 1993, Goodwin and Anthony, 1995). Our understanding of this enzyme has increased dramatically in the last 3 years with publication of the 3-dimensional structures of the enzyme from Methylotrophus W3A1 (at 2.6 Å) (Xia et al., 1992; White et al., 1993) and from Methylobacterium extorquens (at 1.94Å) (Anthony et al., 1994; Ghosh et al., 1995). The system considered in this brief review will be the MDH and cytochrome c L from M. extorquens; in particular, the following questions will be considered: what does the structure tell us about the mechanisms of methanol oxidation, and electron transfer between the two proteins, and the initial interaction (‘docking’) between MDH and cytochrome c L.
KeywordsMethanol Oxidation Prosthetic Group Acetic Acid Bacterium Disulphide Bridge Paracoccus Denitrificans
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