The biosynthetic routes for carbon monoxide and cyanide in the Ni-Fe active site of hydrogenases are different.
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.
Roseboom
Winfried
W
Swammerdam Institute for Life Sciences, University of Amsterdam, Nieuwe Achtergracht 166, NL-1018 WV Amsterdam, The Netherlands.
Blokesch
Melanie
M
Böck
August
A
Albracht
Simon P J
SP
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
D002247:Carbon Isotopes; D003486:Cyanides; D002248:Carbon Monoxide; C043296:nickel-iron hydrogenase; D006864:Hydrogenase