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The biosynthetic routes for carbon monoxide and cyanide in the Ni–Fe active site of hydrogenases are different
Author(s) -
Roseboom Winfried,
Blokesch Melanie,
Böck August,
Albracht Simon P.J.
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.12.013
Subject(s) - cyanide , hydrogenase , carbon monoxide , chemistry , carbon monoxide dehydrogenase , hydrogen cyanide , active site , escherichia coli , enzyme , labelling , biochemistry , combinatorial chemistry , stereochemistry , organic chemistry , catalysis , gene
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.