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Journal Article

Spectroscopic and Computational Evidence that [FeFe] Hydrogenases Operate Exclusively with CO-Bridged Intermediates

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Birrell,  James A.
Research Department DeBeer, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

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Lubitz,  Wolfgang
Research Department Lubitz, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

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DeBeer,  Serena
Research Department DeBeer, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

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Citation

Birrell, J. A., Pelmenschikov, V., Mishra, N., Wang, H., Yoda, Y., Tamasaku, K., et al. (2020). Spectroscopic and Computational Evidence that [FeFe] Hydrogenases Operate Exclusively with CO-Bridged Intermediates. Journal of the American Chemical Society, 142(1), 222-232. doi:10.1021/jacs.9b09745.


Cite as: https://hdl.handle.net/21.11116/0000-0007-8523-B
Abstract
[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.