6SG2

FeFe Hydrogenase from Desulfovibrio desulfuricans in Hinact state

This is a non-PDB format compatible entry.

Summary for 6SG2

• Entry DOI: 10.2210/pdb6sg2/pdb
• Descriptor: Periplasmic [Fe] hydrogenase large subunit, HydB, IRON/SULFUR CLUSTER, ... (5 entities in total)
• Functional Keywords: hydrogenase, iron-sulfur protein, hinact, desulfovibrio desulfuricans, oxidoreductase
• Biological source: Desulfovibrio desulfuricans; More
• Total number of polymer chains: 2
• Total formula weight: 54748.13

Authors

Galle, L.M.,Span, I. (deposition date: 2019-08-02, release date: 2020-07-08, Last modification date: 2024-01-24)

Primary citation

Rodriguez-Macia, P.,Galle, L.M.,Bjornsson, R.,Lorent, C.,Zebger, I.,Yoda, Y.,Cramer, S.P.,DeBeer, S.,Span, I.,Birrell, J.A.
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.
Angew.Chem.Int.Ed.Engl., 59:16786-16794, 2020

PubMed Abstract: [FeFe] hydrogenases are the most active H 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 -stable state called H . To date, the structure and mechanism of formation of H 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 state and its mechanism of formation. This may facilitate the design of O -stable hydrogenases and molecular catalysts.

PubMed: 32488975
DOI: 10.1002/anie.202005208

Experimental method

X-RAY DIFFRACTION (1.65 Å)