期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 109, 期 29, 页码 11516-11521出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1204770109
关键词
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资金
- UK Biotechnology and Biological Sciences Research Council [H003878-1, BB/I022309-1]
- Engineering and Physical Sciences Research Council (EPSRC-Supergen)
- Ministerio de Ciencia e Innovacion [CTQ2010-18570]
- Ministerio de Educacion [PR2010-0466]
- Deutsch Forschungsgemeinschaft [HA 255/2-1]
- BMBF [Bio-H2]
- Volkswagen foundation [LigH2t]
The extraordinary ability of Fe- and Ni-containing enzymes to catalyze rapid and efficient H+/H-2 interconversion-a property otherwise exclusive to platinum metals-has been investigated in a series of experiments combining variable-temperature protein film voltammetry with mathematical modeling. The results highlight important differences between the catalytic performance of [FeFe]-hydrogenases and [NiFe]-hydrogenases and justify a simple model for reversible catalytic electron flow in enzymes and electrocatalysts that should be widely applicable in fields as diverse as electrochemistry, catalysis, and bioenergetics. The active site of [FeFe]-hydrogenases, an intricate Fe-carbonyl complex known as the H cluster, emerges as a supreme catalyst.
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