The Reductive Half-Reaction of MDH

The Role of Ammonia in the Reductive Half-Reaction Mechanism of Methanol Dehydrogenase 

The Oxidative Half-Reaction of Methanoi Dehydrogenase 6.3.1. The iMethanoi Oxidasei Eiectron Transport Chain 

Cytochrome Ch is similar in most respects to other typical bacterial cytochromes c and C2- However its X-ray structure (Read et al., 1999) shows a number of unusual features it bears a closer gross resemblance to mitochondrial cytochrome c than to the bacterial cytochrome C2 and the left hand side of the haem cleft is unique. In particular it is highly hydrophobic, the usual water is absent, and the iconservediTyr67 is replaced by tryptophan. A number of features of the structure demonstrate that the usual hydrogen bonding network involving water in the haem channel is not essential, and that other mechanisms for modulation of redox potentials may exist in this cytochrome. It should be emphasised that the unique character of this cytochrome does not appear to be related in any way to its special involvement in oxidising cytochrome Ci in the methylotroph electron transport chain. 

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