title: Hydrogen evolution from neutral water under aerobic conditions catalyzed by cobalt microperoxidase-11.
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.
authors.affiliation: Department of Chemistry, University of Rochester , Rochester New York 14627-0216, United States.
authors.forename: Jesse G
authors.initials: JG
authors.lastname: Kleingardner
authors.forename: Banu
authors.initials: B
authors.lastname: Kandemir
authors.forename: Kara L
authors.initials: KL
authors.lastname: Bren
mesh_terms: D000332:Aerobiosis; D002384:Catalysis; D003035:Cobalt / Q000737:chemistry*; D006859:Hydrogen / Q000737:chemistry* / Q000378:metabolism; D015394:Molecular Structure; D010544:Peroxidases / Q000378:metabolism*; D014867:Water / Q000737:chemistry*
chemical_list: D014867:Water; D003035:Cobalt; D006859:Hydrogen; D010544:Peroxidases; C021799:microperoxidase