Two alternative substrate paths for compound I formation and reduction in catalase-peroxidase KatG from Burkholderia pseudomallei

Proteins: Structure, Function and Genetics

Volumn 66, Issue 1, 2007, Pages 219-228

  Deemagarn, Taweewat ^a   Wiseman, Ben ^a   Carpena, Xavier ^b   Ivancich, Anabella ^c   Fita, Ignacio ^b   Loewen, Peter C ^a  

^a UNIVERSITY OF MANITOBA   (Canada)

^b INSTITUTE FOR RESEARCH IN BIOMEDICINE   (Spain)

^c CNRS   (France)

Author keywords

Catalase; Crystal structure; Electron paramagnetic resonance; KatG; Peroxidase

Indexed keywords

ALANINE; ARGININE; ASPARTIC ACID; CARBOXYLIC ACID; CATALASE; GLUTAMIC ACID; HEME; HYDROGEN; HYDROGEN PEROXIDE; ISOLEUCINE; KATG PROTEIN; NITROGEN; PEROXIDASE; SOLVENT; WATER;

ACIDITY; AMINO ACID SEQUENCE; ARTICLE; BURKHOLDERIA PSEUDOMALLEI; COVALENT BOND; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; ELECTRON SPIN RESONANCE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SUBSTRATE COMPLEX; ENZYME SYNTHESIS; HYDROGEN BOND; KINETICS; LOW TEMPERATURE; NONHUMAN; PRIORITY JOURNAL; REACTION ANALYSIS; REDUCTION; SEQUENCE ANALYSIS; STRUCTURE ANALYSIS;

BURKHOLDERIA; BURKHOLDERIA PSEUDOMALLEI;

EID: 33845643031     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21209     Document Type: Article

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