期刊
DALTON TRANSACTIONS
卷 50, 期 43, 页码 15754-15759出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/d1dt03295j
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资金
- U.S. Department of Energy (DOE), Office of Science, Office of Basic Energy Sciences (BES), Division of Chemical Sciences, Geosciences Biosciences
- U.S. DOE, Office of Science, Office of Workforce Development for Teachers and Scientists (WDTS) under the Science Undergraduate Laboratory Internships Program (SULI)
- DOE's Office of Biological and Environmental Research
An artificial metalloenzyme was activated by assembling a molecular complex within a structured protein scaffold, showing electrocatalytic hydrogen production activity in a wide pH range. This demonstrates the importance of protein scaffold in enhancing the performance of artificial enzymes.
An artificial metalloenzyme acting as a functional biomimic of hydrogenase enzymes was activated by assembly via covalent attachment of the molecular complex, [Ni((PNP)-P-glycine)(2)](2-), within a structured protein scaffold. Electrocatalytic H-2 production was observed from pH 3.0 to 10.0 for the artificial enzyme, while no electrocatalytic activity was observed for similar [Ni(PNP)(2)](2+) systems.
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