期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 142, 期 1, 页码 222-232出版社
AMER CHEMICAL SOC
DOI: 10.1021/jacs.9b09745
关键词
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资金
- NIH [GM-65440, GM-61153]
- Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) under Germany's Excellence Strategy [EXC 2008/1, 390540038]
- Max Planck Society
- DFG [SPP 1927, DE 1877/1-1, BI 2198/1-1]
- [2018B0141]
- [2018B1379]
[FeFe] hydrogenases are extremely active H-2-converting enzymes. Their mechanism remains highly controversial, in particular, the nature of the one-electron and two-electron reduced intermediates called HredH+ and HsredH+. In one model, the HredH+ and HsredH+ states contain a semibridging CO, while in the other model, the bridging CO is replaced by a bridging hydride. Using low-temperature IR spectroscopy and nuclear resonance vibrational spectroscopy, together with density functional theory calculations, we show that the bridging CO is retained in the HsredH+ and HredH+ states in the [FeFe] hydrogenases from Chlamydomonas reinhardtii and Desulfovibrio desulfuricans, respectively. Furthermore, there is no evidence for a bridging hydride in either state. These results agree with a model of the catalytic cycle in which the HredH+ and HsredH+ states are integral, catalytically competent components. We conclude that proton-coupled electron transfer between the two subclusters is crucial to catalysis and allows these enzymes to operate in a highly efficient and reversible manner.
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