Hydrogen Evolution from Neutral Water under Aerobic Conditions Catalyzed by Cobalt Microperoxidase-11

A molecular electrocatalyst is reported that reduces protons to hydrogen (H2) in neutral water under aerobic conditions. The biomolecular catalyst is made from cobalt substitution of microperoxidase-11, a water-soluble heme-undecapeptide derived from the protein horse cytochrome c. In aqueous soluti...

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Bibliographic Details
Published in:Journal of the American Chemical Society 2014-01, Vol.136 (1), p.4-7
Main Authors: Kleingardner, Jesse G, Kandemir, Banu, Bren, Kara L
Format: Article
Language:English
Subjects:
Aerobiosis
Catalysis
Cobalt - chemistry
Hydrogen - chemistry
Hydrogen - metabolism
Molecular Structure
Peroxidases - metabolism
Water - chemistry
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Summary:A molecular electrocatalyst is reported that reduces protons to hydrogen (H2) in neutral water under aerobic conditions. The biomolecular catalyst is made from cobalt substitution of microperoxidase-11, a water-soluble heme-undecapeptide derived from the protein horse cytochrome c. In aqueous solution at pH 7.0, the catalyst operates with near quantitative Faradaic efficiency, a turnover frequency ∼6.7 s–1 measured over 10 min at an overpotential of 852 mV, and a turnover number of 2.5 × 104. Catalyst activity has low sensitivity to oxygen. The results show promise as a hydrogenase functional mimic derived from a biomolecule.
ISSN:0002-7863
1520-5126
DOI:10.1021/ja406818h