Abstract
The diiron carbonyl cluster is held by a native CXXC motif, which includes Cys14 and Cys17, in the cytochrome c sequence. It is found that the diiron carbonyl complex works well as a catalyst for H(2) evolution. It has a TON of ∼80 over 2 h at pH 4.7 in the presence of a Ru-photosensitizer and ascorbate as a sacrificial reagent in aqueous media.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Catalysis
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Coordination Complexes / chemistry
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Cytochromes c / chemistry*
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Cytochromes c / metabolism
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Hydrogen / chemistry*
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Hydrogen-Ion Concentration
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Hydrogenase / chemistry
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Iron / chemistry
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Iron-Sulfur Proteins / chemistry
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Light
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Models, Molecular*
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Photosensitizing Agents / chemistry
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Ruthenium / chemistry
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Water / chemistry
Substances
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Coordination Complexes
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Iron-Sulfur Proteins
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Photosensitizing Agents
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Water
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Ruthenium
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Hydrogen
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Cytochromes c
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Iron
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iron hydrogenase
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Hydrogenase