title: The biosynthetic routes for carbon monoxide and cyanide in the Ni-Fe active site of hydrogenases are different.
abstract: The incorporation of carbon into the carbon monoxide and cyanide ligands of [NiFe]-hydrogenases has been investigated by using (13)C labelling in infrared studies of the Allochromatium vinosum enzyme and by (14)C labelling experiments with overproduced Hyp proteins from Escherichia coli. The results suggest that the biosynthetic routes of the carbon monoxide and cyanide ligands in [NiFe]-hydrogenases are different.
authors.affiliation: Swammerdam Institute for Life Sciences, University of Amsterdam, Nieuwe Achtergracht 166, NL-1018 WV Amsterdam, The Netherlands.
authors.forename: Winfried
authors.initials: W
authors.lastname: Roseboom
authors.forename: Melanie
authors.initials: M
authors.lastname: Blokesch
authors.forename: August
authors.initials: A
authors.lastname: Böck
authors.forename: Simon P J
authors.initials: SP
authors.lastname: Albracht
mesh_terms: D001665:Binding Sites; D002247:Carbon Isotopes / Q000032:analysis / Q000378:metabolism; D002248:Carbon Monoxide / Q000378:metabolism*; D002841:Chromatiaceae / Q000201:enzymology; D003486:Cyanides / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology; D006864:Hydrogenase / Q000378:metabolism*; D013055:Spectrophotometry, Infrared
chemical_list: D002247:Carbon Isotopes; D003486:Cyanides; D002248:Carbon Monoxide; C043296:nickel-iron hydrogenase; D006864:Hydrogenase