Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1317811 | Journal of Inorganic Biochemistry | 2012 | 4 Pages |
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.
Graphical abstractTo create a [FeFe]-hydrogenase functional model, two essential components, a diiron carbonyl cluster and ruthenium photosensitizer, were attached to the CXXCH peptide platform of the cytochrome c556 sequence. The peptide–metal complex functions as a hydrogen-evolving catalyst with a turnover number of 9 over 2 h in water (pH 8.5).Figure optionsDownload full-size imageDownload as PowerPoint slide