Caught in the H_inact : Crystal Structure and Spectroscopy Reveal a Sulfur Bound to the Active Site of an O₂ -stable State of [FeFe] Hydrogenase.

ABSTRACT: [FeFe] hydrogenases are the most active H₂ 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 O₂ -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 d

SUBMITTER: Rodriguez-Macia P 

PROVIDER: S-EPMC7540559 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature