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

FEBS Letters

Volumn 581, Issue 17, 2007, Pages 3322-3326

  Lenz, Oliver ^a   Zebger, Ingo ^b   Hamann, Josta ^a   Hildebrandt, Peter ^b   Friedrich, Bärbel ^a  

^a HUMBOLDT UNIVERSITY   (Germany)

^b TECHNISCHE UNIVERSITÄT BERLIN   (Germany)

Author keywords

Cyanide; Fourier transform infrared spectroscopy; Iron; Metal carbonyl; Metallocentre assembly; Nickel; Regulatory hydrogenase

Indexed keywords

BACTERIAL PROTEIN; BICARBONATE; CARBAMOYL PHOSPHATE; CARBON DIOXIDE; CITRULLINE; CYANIDE; HYDROGENASE; IRON; LIGAND; NICKEL IRON HYDROGENASE; PROTEIN HYP; UNCLASSIFIED DRUG; UREIDOCITRULLINE C 13;

ARTICLE; BACTERIAL GROWTH; BIOSYNTHESIS; COVALENT BOND; ENZYME ACTIVE SITE; ENZYME PURIFICATION; ESCHERICHIA COLI; INFRARED SPECTROSCOPY; ISOTOPE LABELING; NONHUMAN; PRIORITY JOURNAL; WAUTERSIA EUTROPHA;

BINDING SITES; CARBAMYL PHOSPHATE; CARBON DIOXIDE; CARBON ISOTOPES; CARBON MONOXIDE; CITRULLINE; CLONING, MOLECULAR; CUPRIAVIDUS NECATOR; CYANIDES; HYDROGENASE; PROTEIN SUBUNITS;

CUPRIAVIDUS NECATOR;

EID: 34250851695     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2007.06.027     Document Type: Article

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