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

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Abstract

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.

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

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Publication details

The article was received on 29 Apr 2018, accepted on 14 Sep 2018 and first published on 14 Sep 2018


Article type: Edge Article
DOI: 10.1039/C8SC01948G
Citation: Chem. Sci., 2018, Advance Article
  • Open access: Creative Commons BY license
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    Hydrogen evolution from water catalyzed by cobalt-mimochrome VI*a, a synthetic mini-protein

    V. Firpo, J. M. Le, V. Pavone, A. Lombardi and K. L. Bren, Chem. Sci., 2018, Advance Article , DOI: 10.1039/C8SC01948G

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