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Functional roles of the heme architecture and its environment in tetraheme cytochrome C.

Cytochromes are involved in a wide variety of redox reactions in living systems. Some of them contain multiple hemes such as Desulfovibrio cytochrome c3 and Shewanella small tetraheme cytochrome c. The significance of c-type tetraheme architectures was discussed. A cyclic heme architecture and its environment regulate the extremely low redox potentials of cytochrome c3 in addition to bis-imidazole coordination and heme exposure. Each heme in cytochrome c3 plays a different role in the electron transport to/from [NiFe] hydrogenase and the specific CO-binding. In contrast, the chain-like heme architecture in Shewanella small tetraheme cytochrome c and soluble fumarate reductase provides a pathway for directional electron transfer. Thus, the tetraheme architectures do not comprise simple heme assemblies but sophisticated devices.[1]

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