Electron Transfer Regulation in Tetraheme Cytochromes Revealed by NMR 北京大学纳米科技论坛系列报告之118讲 Electron Transfer Regulation in Tetraheme Cytochromes Revealed by NMR 报告人: Prof. Hideo Akutsu Osaka University Yokohama City University 地 点：北京大学化学学院A717学术报告厅 时 间：2019年05月13日(星期一) 上午10:00 主请人：刘忠范 院士 Abstract： Cytochromes are ubiquitous heme-proteins that are involved in a wide variety of redox reactions in biological electron transport systems. Some cytochromes have multiple hemes, generally protoporphyrins coordinated to iron. They are mainly found in bacteria that can be traced back more than 500 million years to the anaerobic world, and reveal special redox features because of heme-heme interactions. Such features will be discussed in this talk focusing on c-type tetraheme-cytochromes. A cyclic heme architecture and its environment including bis-imidazole coordination and heme exposure realize extremely low redox potentials of cytochrome c3. To elucidate its mechanism, the effect of extensive mutations at conserved and non-conserved aromatic residues on the coordination property of heme irons was investigated, using NMR and X-ray crystallography. The results suggested the importance of p-p interaction and p-cation interactions among hemes and conserved aromatic rings. On determination of heme reduction potentials, each heme in cytochrome c3 was expected to play a different role in the electron transport with other redox proteins. It was supported by the interaction with [NiFe] hydrogenase. Design of the heme architecture is also important. In contrast to cytochrome c3, the chain-like heme architecture in Shewanella small tetraheme cytochrome c provides a pathway for directional electron transfer. Actually, soluble fumarate reductase visualizes a directional electron transfer through a molecular wire. Thus, the tetraheme architectures can work as sophisticated devices. 欢 迎 参 加