The cytochrome bd-type quinol oxidase is important for survival of Mycobacterium smegmatis under peroxide and antibiotic-induced stress

Scientific Reports

Volumn 5, Issue , 2015, Pages

  Lu, Ping ^a   Heineke, Marieke H ^a   Koul, Anil ^b   Andries, Koen ^b   Cook, Gregory M ^c   Lill, Holger ^a   Van Spanning, Rob ^a   Bald, Dirk ^a  

^a AMSTERDAM INSTITUTE FOR MOLECULES   (Netherlands)

^b JANSSEN RESEARCH AND DEVELOPMENT   (Belgium)

^c UNIVERSITY OF OTAGO   (New Zealand)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIINFECTIVE AGENT; AURACHIN D; BACTERIAL PROTEIN; BEDAQUILINE; CLOFAZIMINE; CYTOCHROME C OXIDASE; HYDROGEN PEROXIDE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE; QUINOLINE DERIVATIVE; QUINOLONE DERIVATIVE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE;

ANTAGONISTS AND INHIBITORS; CHEMISTRY; DRUG EFFECTS; ENZYMOLOGY; GENE INACTIVATION; GENETICS; METABOLISM; MUTATION; MYCOBACTERIUM SMEGMATIS; PHYSIOLOGICAL STRESS;

ANTI-BACTERIAL AGENTS; ATP SYNTHETASE COMPLEXES; BACTERIAL PROTEINS; CLOFAZIMINE; DIARYLQUINOLINES; ELECTRON TRANSPORT COMPLEX IV; GENE KNOCKOUT TECHNIQUES; HYDROGEN PEROXIDE; MUTATION; MYCOBACTERIUM SMEGMATIS; NADH DEHYDROGENASE; QUINOLONES; REACTIVE OXYGEN SPECIES; STRESS, PHYSIOLOGICAL;

EID: 84934881033     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep10333     Document Type: Article

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