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Structure paper

TitleAccumulating the hydride state in the catalytic cycle of [FeFe]-hydrogenases.
Journal, issue, pagesNat Commun, Vol. 8, Page 16115-16115, Year 2017
Publish dateJun 13, 2016 (structure data deposition date)
AuthorsWinkler, M. / Senger, M. / Duan, J. / Esselborn, J. / Wittkamp, F. / Hofmann, E. / Apfel, U.P. / Stripp, S.T. / Happe, T.
External linksNat Commun / PubMed:28722011
MethodsX-ray diffraction
Resolution2.29 Å
Structure data

PDB-5la3:
[FeFe]-hydrogenase CpI from Clostridium pasteurianum, variant E279A
Method: X-RAY DIFFRACTION / Resolution: 2.29 Å

Chemicals

ChemComp-402:
dicarbonyl[bis(cyanide-kappaC)]-mu-(iminodimethanethiolatato-1kappaS:2kappaS)-mu-(oxomethylidene)diiron(2+)

ChemComp-SF4:
IRON/SULFUR CLUSTER

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

Source
  • clostridium pasteurianum (bacteria)
KeywordsOXIDOREDUCTASE / Hydrogenase / H-cluster / semisynthetic enzyme

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