Photocatalytic hydrogen evolution by a diiron hydrogenase model based on a peptide fragment of cytochrome c₅₅₆ with an attached diiron carbonyl cluster and an attached ruthenium photosensitizer

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• 作者：Yohei Sano^a ; Akira Onoda^a ; ^b ; Takashi Hayashi^a ; ^{thayashi@chem.eng.osaka-u.ac.jp}
• 关键词：Diiron carbonyl cluster ; Cytochrome c556 ; Photocatalytic hydrogen evolution ; Intramolecular electron transfer system
• 刊名：Journal of Inorganic Biochemistry
• 出版年：2012
• 期刊代码：53_01620134
• 类别：ch
• 出版时间：March, 2012
• 卷：108
• 期：Complete
• 页码：159-162
• 文件大小：539 K

摘要

It is of particular interest to mimic the process of intramolecular electron relay at the active site of [FeFe]-hydrogenase in order to understand the mechanism of the catalytic activity of H₂ evolution. We have recently focused on using the native CXXCH peptide sequence of the C-terminal segment of cytochrome c₅₅₆ as a platform which holds a diiron carbonyl cluster via two cysteines and have attached a ruthenium photosensitizer via a histidine. The modified peptide with the two metal moieties is found to act as the photocatalyst for H₂ evolution with a turnover number of ~ 9 over 2 h at pH 8.5 in the presence of ascorbate as a sacrificial reagent.