A low-spin iron with CN and CO as intrinsic ligands forms the core of the active site in [Fe]-hydrogenases

European Journal of Biochemistry

Volumn 258, Issue 2, 1998, Pages 572-578

  Pierik, Antonio J ^a   Hulstein, Marco ^b   Hagen, Wilfred R ^b   Albracht, Simon P J ^a  

^a UNIVERSITY OF AMSTERDAM   (Netherlands)

^b WAGENINGEN UNIVERSITY   (Netherlands)

Author keywords

Active site; Carbon monoxide; Cyanide; Hydrogenase; Iron

Indexed keywords

CARBON MONOXIDE; CYANIDE; FERRIC ION; HYDROGENASE; IRON; LIGAND; SULFUR;

ARTICLE; CHROMATIUM VINOSUM; DESULFOVIBRIO VULGARIS; ENZYME ACTIVE SITE; INFRARED RADIATION; NONHUMAN; OXIDATION REDUCTION STATE; PRIORITY JOURNAL;

BACTERIAL PROTEINS; BINDING SITES; DESULFOVIBRIO VULGARIS; ELECTRON SPIN RESONANCE SPECTROSCOPY; HYDROGEN; HYDROGENASE; IRON-SULFUR PROTEINS; MOLECULAR STRUCTURE; NONHEME IRON PROTEINS; OXIDATION-REDUCTION; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

ALLOCHROMATIUM VINOSUM; CHROMATIUM; DESULFOVIBRIO VULGARIS;

EID: 0032403791     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2580572.x     Document Type: Article

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