Defects in a quinol oxidase lead to loss of KatC catalase activity in Pseudomonas aeruginosa: KatC activity is temperature dependent and it requires an intact disulphide bond formation system

Biochemical and Biophysical Research Communications

Volumn 341, Issue 3, 2006, Pages 697-702

  Mossialos, Dimitris ^a   Tavankar, Gholam Reza ^a   Zlosnik, James E A ^a   Williams, Huw D ^a  

^a IMPERIAL COLLEGE LONDON   (United Kingdom)

Author keywords

Catalase; Cytochrome bd; Disulphide bond; DsbA; Oxidative stress; Respiration

Indexed keywords

CATALASE; ELASTASE; HYDROGEN PEROXIDE; KATC ENZYME; OXIDOREDUCTASE; TRIACYLGLYCEROL LIPASE; UNCLASSIFIED DRUG;

ARTICLE; DISULFIDE BOND; ENZYME ACTIVITY; ENZYME LOCALIZATION; ENZYME MECHANISM; NONHUMAN; OXIDATION REDUCTION STATE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PSEUDOMONAS AERUGINOSA; TEMPERATURE DEPENDENCE;

CATALASE; DISULFIDES; GENE EXPRESSION REGULATION, ENZYMOLOGIC; MUTATION; OXIDATION-REDUCTION; OXIDOREDUCTASES; PROTEIN DISULFIDE-ISOMERASE; PSEUDOMONAS AERUGINOSA; REACTIVE OXYGEN SPECIES; TEMPERATURE; TRANSCRIPTION, GENETIC;

BACTERIA (MICROORGANISMS); PSEUDOMONAS AERUGINOSA;

EID: 31744440140     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.12.225     Document Type: Article

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