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Journal Article

MvhB-type Polyferredoxin as an Electron-transfer Chain in Putative Redox-enzyme Complexes

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Watanabe,  Tomohiro
Department-Independent Research Group Microbial Protein Structure, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Shima,  Seigo
Department-Independent Research Group Microbial Protein Structure, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Citation

Watanabe, T., & Shima, S. (2021). MvhB-type Polyferredoxin as an Electron-transfer Chain in Putative Redox-enzyme Complexes. CHEMISTRY LETTERS, 50(2), 353-360. doi:10.1246/cl.200774.


Cite as: https://hdl.handle.net/21.11116/0000-0009-4BC6-4
Abstract
Ferredoxin is a type of electron carrier protein involved in many biological redox reactions and also incorporated as an electron transfer domain and subunit in redox enzyme complexes. MvhB-type polyferredoxin is an iron-sulphur protein composed of three to seven 2[4Fe-4S]-ferredoxin domains. In this short review, we introduce the structure and function of MvhB-type polyferredoxin modules in methanogenic enzymes and then discuss the possible physiological function of the putative MvhB-like polyferredoxins identified in microbial genomes.