Abstract
Type I cytochrome c 3 is a key protein in the bioenergetic metabolism of Desulfovibrio spp., mediating electron transfer between periplasmic hydrogenase and multihaem cytochromes associated with membrane bound complexes, such as type II cytochrome c 3. This work presents the NMR assignment of the haem substituents in type I cytochrome c 3 isolated from Desulfovibrio africanus and the thermodynamic and kinetic characterisation of type I and type II cytochromes c 3 belonging to the same organism. It is shown that the redox properties of the two proteins allow electrons to be transferred between them in the physiologically relevant direction with the release of energised protons close to the membrane where they can be used by the ATP synthase.
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