期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 54, 期 24, 页码 7110-7113出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201502338
关键词
biocatalysis; electrochemistry; hydrogenase; in situ spectroscopy; IR spectroscopy
资金
- European Research Council [EnergyBioCatalysis-ERC-2010-StG-258600)]
- Biotechnology and Biological Sciences Research Council [BB/L009722/1]
- Engineering and Physical Sciences Research Council [EP/K031503/1]
- Ministerio de Ciencia y Tecnologia
- Universidad de Costa Rica
- Lincoln College, Oxford
- EPSRC [EP/K031503/1] Funding Source: UKRI
- Engineering and Physical Sciences Research Council [EP/K031503/1] Funding Source: researchfish
A novel in situ IR spectroscopic approach is demonstrated for the characterization of hydrogenase during catalytic turnover. E. coli hydrogenase 1 (Hyd-1) is adsorbed on a high surface-area carbon electrode and subjected to the same electrochemical control and efficient supply of substrate as in protein film electrochemistry during spectral acquisition. The spectra reveal that the active site state known as Ni-L, observed in other NiFe hydrogenases only under illumination or at cryogenic temperatures, can be generated reversibly in the dark at ambient temperature under both turnover and nonturnover conditions. The observation that Ni-L is present at all potentials during turnover under H-2 suggests that the final steps in the catalytic cycle of H-2 oxidation by Hyd-1 involve sequential proton and electron transfer via Ni-L. A broadly applicable IR spectroscopic technique is presented for addressing electrode-adsorbed redox enzymes under fast catalytic turnover.
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