The cytochrome bd quinol oxidase in Escherichia coli has an extremely high oxygen affinity and two oxygen-binding haems: Implications for regulation of activity in vivo by oxygen inhibition

Microbiology

Volumn 142, Issue 4, 1996, Pages 755-763

  D'Mello, Rita ^a   Hill, Susan ^b   Poole, Robert K ^a  

^a KING'S COLLEGE LONDON   (United Kingdom)

^b UNIVERSITY OF SUSSEX   (United Kingdom)

Author keywords

Cytochromes; Escherichia coli; Oxygen affinity; Quinol oxidases; Respiratory electron flux

Indexed keywords

CYTOCHROME B; CYTOCHROME D; HEME; OXIDOREDUCTASE; OXYGEN; OXYHEMOGLOBIN;

ARTICLE; CELL RESPIRATION; CONTROLLED STUDY; ELECTRON TRANSPORT; ENZYME ACTIVITY; ENZYME REGULATION; ESCHERICHIA COLI; KINETICS; NONHUMAN; OXYGEN AFFINITY; PRIORITY JOURNAL; TRANSCRIPTION REGULATION;

ESCHERICHIA COLI;

EID: 0029981912     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/00221287-142-4-755     Document Type: Article

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