Title

Hydrogen evolution from neutral water under aerobic conditions catalyzed by cobalt microperoxidase-11

Document Type

Article

Publication Date

1-8-2014

Abstract

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 × 10 4. Catalyst activity has low sensitivity to oxygen. The results show promise as a hydrogenase functional mimic derived from a biomolecule. © 2013 American Chemical Society.

Comments

Kleingardner, J. G., Kandemir, B., & Bren, K. L. (2014). Hydrogen evolution from neutral water under aerobic conditions catalyzed by cobalt microperoxidase-11. Journal of the American Chemical Society, 136(1), 4–7. https://doi.org/10.1021/ja406818h

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