期刊
JOURNAL OF INORGANIC BIOCHEMISTRY
卷 108, 期 -, 页码 159-162出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.jinorgbio.2011.07.010
关键词
Diiron carbonyl cluster; Cytochrome c(556); Photocatalytic hydrogen evolution; Intramolecular electron transfer system
资金
- MEXT
- Japan Society for the Promotion of Science (JSPS)
- Research Fellowships for Young Scientists
- Osaka University
- Frontier Research Base for Global Young Researchers, Osaka University, MEXT
- Grants-in-Aid for Scientific Research [22105013, 23655050, 22655017, 22108518, 10J00580] Funding Source: KAKEN
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 H-2 evolution. We have recently focused on using the native CXXCH peptide sequence of the C-terminal segment of cytochrome c(556) 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 H-2 evolution with a turnover number of similar to 9 over 2 h at pH 8.5 in the presence of ascorbate as a sacrificial reagent. (c) 2011 Elsevier Inc. All rights reserved.
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