The biosynthetic routes for carbon monoxide and cyanide in the Ni–Fe active site of hydrogenases are different | Zendy

Roseboom Winfried | Zendy; Blokesch Melanie | Zendy; Böck August | Zendy; Albracht Simon P.J. | Zendy

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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.

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