Abstract
[FeFe] hydrogenases are highly efficient catalysts for reversible dihydrogen evolution. H2 turnover involves different catalytic intermediates including a recently characterized hydride state of the active site (H-cluster). Applying cryogenic infrared and electron paramagnetic resonance spectroscopy to an [FeFe] model hydrogenase from Chlamydomonas reinhardtii (CrHydA1), we have discovered two new hydride intermediates and spectroscopic evidence for a bridging CO ligand in two reduced H-cluster states. Our study provides novel insights into these key intermediates, their relevance for the catalytic cycle of [FeFe] hydrogenase, and novel strategies for exploring these aspects in detail.
Original language | English |
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Pages (from-to) | 5493-5497 |
Number of pages | 5 |
Journal | Journal of the American Chemical Society |
Volume | 142 |
Issue number | 12 |
Early online date | 3 Mar 2020 |
DOIs | |
Publication status | Published - 25 Mar 2020 |