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Title: Hydrogen evolution from water catalyzed by cobalt-mimochrome VI*a, a synthetic mini-protein

Journal Article · · Chemical Science
DOI:https://doi.org/10.1039/C8SC01948G· OSTI ID:1471784

A synthetic enzyme is reported that electrocatalytically reduces protons to hydrogen (H2) in water near neutral pH under aerobic conditions. Cobalt mimochrome VI*a (CoMC6*a) is a mini-protein with a cobalt deuteroporphyrin active site within a scaffold of two synthetic peptides covalently bound to the porphyrin. Comparison of the activity of CoMC6*a to that of cobalt microperoxidase-11 (CoMP11-Ac), a cobalt porphyrin catalyst with a single “proximal” peptide and no organized secondary structure, reveals that CoMC6*a has significantly enhanced longevity, yielding a turnover number exceeding 230 000, in comparison to 25 000 for CoMP11-Ac. Furthermore, comparison of cyclic voltammograms of CoMC6*a and CoMP11-Ac indicates that the trifluoroethanol-induced folding of CoMC6*a lowers the overpotential for catalytic H2 evolution by up to 100 mV. These results demonstrate that even a minimal polypeptide matrix can enhance longevity and efficiency of a H2-evolution catalyst.

Research Organization:
Univ. of Rochester, NY (United States)
Sponsoring Organization:
USDOE Office of Science (SC), Basic Energy Sciences (BES)
Grant/Contract Number:
FG02-09ER16121; SC0002106
OSTI ID:
1471784
Alternate ID(s):
OSTI ID: 1610622
Journal Information:
Chemical Science, Journal Name: Chemical Science Vol. 9 Journal Issue: 45; ISSN 2041-6520
Publisher:
Royal Society of ChemistryCopyright Statement
Country of Publication:
United Kingdom
Language:
English
Citation Metrics:
Cited by: 51 works
Citation information provided by
Web of Science

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