Roles for Arg426 and Trp111 in the modulation of NADH oxidase activity of the catalase-peroxidase KatG from Burkholderia pseudomallei inferred from pH-induced structural changes

Biochemistry

Volumn 45, Issue 16, 2006, Pages 5171-5179

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

^a INSTITUT DE BIOLOGIA MOLECULAR DE BARCELONA   (Spain)

^b UNIVERSITY OF MANITOBA   (Canada)

^c CNRS   (France)

Author keywords

[No Author keywords available]

Indexed keywords

CRYSTAL STRUCTURE; ENZYMES; MOLECULAR STRUCTURE; OPTICAL RESOLVING POWER; PH EFFECTS; PROTEINS; X RAY DIFFRACTION ANALYSIS;

BURKHOLDERIA PSEUDOMALLEI; MOLECULAR OXYGEN; PERHYDROXY GROUPS; PROTONATION;

ENZYME KINETICS;

ARGININE; HEME; HISTIDINE; INDOLE; KATG PROTEIN; METHIONINE; NITROGEN; OXYGEN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; SERINE; THREONINE; TRYPTOPHAN;

ARTICLE; BURKHOLDERIA PSEUDOMALLEI; ELECTRON SPIN RESONANCE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME CONFORMATION; LOW TEMPERATURE; NONHUMAN; PH; PRIORITY JOURNAL; PROTON TRANSPORT;

BURKHOLDERIA PSEUDOMALLEI;

EID: 33645996688     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi060017f     Document Type: Article

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