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Structure paper

TitleDioxygen Sensitivity of [Fe]-Hydrogenase in the Presence of Reducing Substrates.
Journal, issue, pagesAngew. Chem. Int. Ed. Engl., Vol. 57, Page 4917-4920, Year 2018
Publish dateJul 25, 2017 (structure data deposition date)
AuthorsHuang, G. / Wagner, T. / Ermler, U. / Bill, E. / Ataka, K. / Shima, S.
External linksAngew. Chem. Int. Ed. Engl. / PubMed:29462510
MethodsX-ray diffraction
Resolution1.29 Å
Structure data

PDB-5ok4:
Crystal structure of native [Fe]-hydrogenase Hmd from Methanothermobacter marburgensis inactivated by O2.
Method: X-RAY DIFFRACTION / Resolution: 1.29 Å

Chemicals

ChemComp-FE:
Unknown entry

ChemComp-FEG:
5'-O-[(S)-{[2-(carboxymethyl)-6-hydroxy-3,5-dimethylpyridin-4-yl]oxy}(hydroxy)phosphoryl]guanosine

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • methanothermobacter marburgensis str. marburg (archaea)
KeywordsOXIDOREDUCTASE / [Fe]-hydrogenase / Fe-Guanylylpyridinol cofactor / H2 / hydrogenase / methanogenesis / methenyl-tetrahydromethanopterin / methylene-tetrahydromethanopterin / hydrogenation / O2 / inactivation

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