6sg2

Publication Abstract from PubMed

[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 A 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.

Caught in the Hinact: Crystal Structure and Spectroscopy Reveal a Sulfur Bound to the Active Site of an O2-stable State of [FeFe] Hydrogenase.,Rodriguez-Macia P, Galle L, Bjornsson R, Lorent C, Zebger I, Yoda Y, Cramer S, DeBeer S, Span I, Birrell J Angew Chem Int Ed Engl. 2020 Jun 2. doi: 10.1002/anie.202005208. PMID:32488975^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.