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Structure paper

TitleHydrogen activation by NiFe-hydrogenases - consolidating the role of the pendant arginine.
Journal, issue, pagesTo Be Published
Publish dateSep 30, 2019 (structure data deposition date)
AuthorsBeaton, S.E. / Evans, R.M. / Kertess, L. / Carr, S.B. / Armstrong, F.A.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution1.2 - 1.5 Å
Structure data

PDB-6syo:
Hydrogenase-2 variant R479K - As Isolated form
Method: X-RAY DIFFRACTION / Resolution: 1.25 Å

PDB-6syx:
Hydrogenase-2 variant R479K - reduced sample exposed to pure oxygen
Method: X-RAY DIFFRACTION / Resolution: 1.3 Å

PDB-6szd:
Hydrogenase-2 variant R479K - hydrogen reduced form
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-6szk:
Hydrogenase-2 variant R479K - hydrogen reduced form treated with CO
Method: X-RAY DIFFRACTION / Resolution: 1.2 Å

Chemicals

ChemComp-SF4:
IRON/SULFUR CLUSTER

ChemComp-F3S:
FE3-S4 CLUSTER

ChemComp-GOL:
GLYCEROL

ChemComp-FCO:
CARBONMONOXIDE-(DICYANO) IRON

ChemComp-NI:
NICKEL (II) ION

ChemComp-MG:
Unknown entry

ChemComp-OXY:
OXYGEN MOLECULE

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

ChemComp-CMO:
CARBON MONOXIDE

Source
  • escherichia coli (E. coli)
  • escherichia coli (strain k12) (bacteria)
  • escherichia coli k-12 (bacteria)
  • escherichia coli 908519 (bacteria)
KeywordsOXIDOREDUCTASE / [NiFe]-hydrogenase / iron-sulphur clusters

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