期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 54, 期 42, 页码 12303-12307出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201502364
关键词
enzyme catalysis; hydrogen oxidation; hydrogenases; molecular catalysis; surface-immobilized catalysis
资金
- Max Planck Society
- Cluster of Excellence RESOLV - Deutsche Forschungsgemeinschaft (DFG) [EXC1069]
- Office of Science Early Career Research Program through the US Department of Energy (US DOE), Office of Science, Office of Basic Energy Sciences (BES)
The active site of hydrogenases has been a source of inspiration for the development of molecular catalysts. However, direct comparisons between molecular catalysts and enzymes have not been possible because different techniques are used to evaluate both types of catalysts, minimizing our ability to determine how far we have come in mimicking the enzymatic performance. The catalytic properties of the [Ni((P2N2Gly)-N-Cy)(2)](2+) complex with the [NiFe]-hydrogenase from Desulfovibrio vulgaris immobilized on a functionalized electrode were compared under identical conditions. At pH 7, the enzyme shows higher activity and lower overpotential with better stability, while at low pH, the molecular catalyst outperforms the enzyme in all respects. This is the first direct comparison of enzymes and molecular complexes, enabling a unique understanding of the benefits and detriments of both systems, and advancing our understanding of the utilization of these bio-inspired complexes in fuel cells.
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