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TitleProbing Ferryl Reactivity in a Nonheme Iron Oxygenase Using an Expanded Genetic Code.
Journal, issue, pagesAcs Catalysis, Vol. 14, Page 11584-11590, Year 2024
Publish dateMar 21, 2024 (structure data deposition date)
AuthorsHardy, F.J. / Quesne, M.G. / Gerard, E.F. / Zhao, J. / Ortmayer, M. / Taylor, C.J. / Ali, H.S. / Slater, J.W. / Levy, C.W. / Heyes, D.J. ...Hardy, F.J. / Quesne, M.G. / Gerard, E.F. / Zhao, J. / Ortmayer, M. / Taylor, C.J. / Ali, H.S. / Slater, J.W. / Levy, C.W. / Heyes, D.J. / Bollinger Jr., J.M. / de Visser, S.P. / Green, A.P.
External linksAcs Catalysis / PubMed:39114090
MethodsX-ray diffraction
Resolution1.6 Å
Structure data

PDB-9eqf:
Crystal structure of the L-arginine hydroxylase VioC MeHis316, bound to Fe(II), L-arginine, and succinate
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

Chemicals

ChemComp-FE2:
Unknown entry

ChemComp-SIN:
SUCCINIC ACID

ChemComp-ARG:
ARGININE

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-HOH:
WATER

Source
  • synthetic construct (others)
KeywordsOXIDOREDUCTASE / non canonical amino acid / hydroxylate / 2OG oxygenase

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