Implications for the Catalytic Mechanism of the Vanadium-Containing Enzyme Chloroperoxidase from the Fungus Curvularia inaequalis by X-Ray Structures of the Native and Peroxide Form

Biological Chemistry

Volumn 378, Issue 3-4, 1997, Pages 309-316

  Messerschmidt, Albrecht ^a   Prade, Lars ^a   Wever, Ron ^b  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

^b UNIVERSITY OF AMSTERDAM   (Netherlands)

Author keywords

Chloroperoxidase; Native form; Peroxide binding; Vanadium coordination; Vanadium enzyme; X Ray structure

Indexed keywords

CHLORIDE PEROXIDASE; FUNGAL ENZYME; HISTIDINE; MICROBIAL ENZYME; NITROGEN; OXYGEN; UNCLASSIFIED DRUG; VANADIUM;

ARTICLE; CRYSTAL STRUCTURE; ENZYME MECHANISM; ENZYME STRUCTURE; FOURIER TRANSFORMATION; FUNGUS; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL;

BINDING SITES; CATALYSIS; CHLORIDE PEROXIDASE; CRYSTALLOGRAPHY, X-RAY; FOURIER ANALYSIS; HYDROGEN BONDING; MITOSPORIC FUNGI; MODELS, MOLECULAR; PEROXIDES; PROTEIN CONFORMATION; VANADIUM COMPOUNDS;

CURVULARIA INAEQUALIS; FUNGI;

EID: 0030906620     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/bchm.1997.378.3-4.309     Document Type: Article

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