Cofactor and substrate binding to vanadium chloroperoxidase determined by UV - VIS spectroscopy and evidence for high affinity for pervanadate

Biochemistry

Volumn 39, Issue 5, 2000, Pages 1133-1141

  Renirie, Rokus ^a   Hemrika, Wieger ^a   Piersma, Sander R ^b   Wever, Ron ^a  

^a UNIVERSITY OF AMSTERDAM   (Netherlands)

^b WAGENINGEN UNIVERSITY   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

CHLORIDE PEROXIDASE; PERVANADATE; VANADIUM DERIVATIVE;

ARTICLE; ENZYME SUBSTRATE COMPLEX; FUNGUS; MOLECULAR INTERACTION; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; ULTRAVIOLET SPECTROSCOPY;

APOENZYMES; ASCOMYCOTA; BINDING SITES; CHLORIDE PEROXIDASE; HYDROGEN PEROXIDE; HYDROGEN-ION CONCENTRATION; KINETICS; MUTAGENESIS, SITE-DIRECTED; RECOMBINANT PROTEINS; SPECTROPHOTOMETRY, ULTRAVIOLET; SUBSTRATE SPECIFICITY; VANADATES; VANADIUM;

FUNGI;

EID: 0034620587     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi9921790     Document Type: Article

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