Journal
ACCOUNTS OF CHEMICAL RESEARCH
Volume 40, Issue 3, Pages 171-178Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ar030262g
Keywords
-
Categories
Ask authors/readers for more resources
Cytochromes are involved in a wide variety of redox reactions in living systems. Some of them contain multiple hemes such as Desulfovibrio cytochrome c(3) 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 c(3) in addition to bis-imidazole coordination and heme exposure. Each heme in cytochrome c(3) 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available