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Carbamoylphosphate serves as the source of CN-, but not of the intrinsic CO in the active site of the regulatory [NiFe]-hydrogenase from Ralstonia eutropha
Zitatschlüssel Lenz2007
Autor Lenz, O. and Zebger, I. and Hamann, J. and Hildebrandt, P. and Friedrich, B.
Seiten 3322–3326
Jahr 2007
Journal Febs Letters
Jahrgang 581
Nummer 17
Zusammenfassung Within the catalytic centre of [NiFe]-hydrogenases one carbonyl and two cyanide ligands are covalently attached to the iron. To identify the metabolic origins of these ligands, the regulatory [NiFe] hydrogenase in conjunction with the indigenous Hyp maturation proteins of Ralstonia eutropha H16 were heterologously overproduced in E. coli grown in the presence of L-[ureido-C-13] citrulline and (NaHCO3)-C-13. Infrared spectroscopy of purified hydrogenase provided direct evidence that only the cyanide ligands, but not the CO ligand, originate from CO2 and carbamoylphosphate. Incorporation of label from (CO)-C-13 exclusively into the carbonyl ligand indicates that free CO is a possible precursor in carbonyl ligand biosynthesis. (C) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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