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 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.
Kleingardner, Jesse G.; Kandemir, Banu; and Bren, Kara L., "Hydrogen evolution from neutral water under aerobic conditions catalyzed by cobalt microperoxidase-11" (2014). Educator Scholarship. 12.