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TitleBinding of exogenous cyanide reveals new active-site states in [FeFe] hydrogenases.
Journal, issue, pagesChem Sci, Vol. 14, Page 2826-2838, Year 2023
Publish dateNov 3, 2022 (structure data deposition date)
AuthorsMartini, M.A. / Bikbaev, K. / Pang, Y. / Lorent, C. / Wiemann, C. / Breuer, N. / Zebger, I. / DeBeer, S. / Span, I. / Bjornsson, R. ...Martini, M.A. / Bikbaev, K. / Pang, Y. / Lorent, C. / Wiemann, C. / Breuer, N. / Zebger, I. / DeBeer, S. / Span, I. / Bjornsson, R. / Birrell, J.A. / Rodriguez-Macia, P.
External linksChem Sci / PubMed:36937599
MethodsX-ray diffraction
Resolution1.01 - 1.04 Å
Structure data

PDB-8bj7:
Desulfovibrio desulfuricans FeFe Hydrogenase C178A mutant in Hinact-like state
Method: X-RAY DIFFRACTION / Resolution: 1.04 Å

PDB-8bj8:
Desulfovibrio desulfuricans FeFe Hydrogenase C178A mutant in Htrans-like state
Method: X-RAY DIFFRACTION / Resolution: 1.01 Å

Chemicals

ChemComp-SF4:
IRON/SULFUR CLUSTER

ChemComp-VHR:
Binuclear [FeFe], di(thiomethyl)amine, carbon monoxide, cyanide cluster (-CN form)

ChemComp-HOH:
WATER

Source
  • desulfovibrio desulfuricans (bacteria)
KeywordsOXIDOREDUCTASE / [FeFe] Hydrogenase / C178A mutant

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