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Caught in the H inact : Crystal Structure and Spectroscopy Reveal a Sulfur Bound to the Active Site of an O 2 ‐stable State of [FeFe] Hydrogenase
Author(s) -
RodríguezMaciá Patricia,
Galle Lisa M.,
Bjornsson Ragnar,
Lorent Christian,
Zebger Ingo,
Yoda Yoshitaka,
Cramer Stephen P.,
DeBeer Serena,
Span Ingrid,
Birrell James A.
Publication year - 2020
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.202005208
Subject(s) - resonance raman spectroscopy , raman spectroscopy , hydrogenase , infrared spectroscopy , spectroscopy , chemistry , active site , crystallography , x ray absorption spectroscopy , sulfur , photochemistry , absorption spectroscopy , crystal structure , catalysis , oxidation state , physics , organic chemistry , quantum mechanics , optics
[FeFe] hydrogenases are the most active H 2 converting catalysts in nature, but their extreme oxygen sensitivity limits their use in technological applications. The [FeFe] hydrogenases from sulfate reducing bacteria can be purified in an O 2 ‐stable state called H inact . To date, the structure and mechanism of formation of H inact remain unknown. Our 1.65 Å crystal structure of this state reveals a sulfur ligand bound to the open coordination site. Furthermore, in‐depth spectroscopic characterization by X‐ray absorption spectroscopy (XAS), nuclear resonance vibrational spectroscopy (NRVS), resonance Raman (RR) spectroscopy and infrared (IR) spectroscopy, together with hybrid quantum mechanical and molecular mechanical (QM/MM) calculations, provide detailed chemical insight into the H inact state and its mechanism of formation. This may facilitate the design of O 2 ‐stable hydrogenases and molecular catalysts.