Caught in the Hinact : Crystal Structure and Spectroscopy Reveal a Sulfur Bound to the Active Site of an O2 -stable State of [FeFe] Hydrogenase.
Angew Chem Int Ed Engl
; 59(38): 16786-16794, 2020 09 14.
Article
en En
| MEDLINE
| ID: mdl-32488975
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 Hinact . To date, the structure and mechanism of formation of Hinact remain unknown. Our 1.65â
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 Hinact state and its mechanism of formation. This may facilitate the design of O2 -stable hydrogenases and molecular catalysts.
Palabras clave
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Oxígeno
/
Azufre
/
Clostridium beijerinckii
/
Hidrógeno
/
Hidrogenasas
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Proteínas Hierro-Azufre
Idioma:
En
Año:
2020
Tipo del documento:
Article