Escherichia coli flavohaemoglobin (Hmp) reduces cytochrome c and Fe(III)-hydroxamate K by electron transfer from NADH via FAD: Sensitivity of oxidoreductase activity to haem-bound dioxygen

Microbiology

Volumn 143, Issue 5, 1997, Pages 1557-1565

  Poole, Robert K ^a,c   Rogers, Nicola J ^a   D'Mello, Rita A M ^a,d   Hughes, Martin N ^a   Orii, Yutaka ^b  

^a KING'S COLLEGE LONDON   (United Kingdom)

^b KYOTO UNIVERSITY   (Japan)

^c UNIVERSITY OF SHEFFIELD   (United Kingdom)

^d IMPERIAL COLLEGE LONDON   (United Kingdom)

Author keywords

Escherichia coli; Haemoglobin (bacterial); Hmp; NADH cytochrome c oxidoreductase; Oxygen sensor

Indexed keywords

CARBON MONOXIDE; CYTOCHROME C; FLAVINE ADENINE NUCLEOTIDE; FLAVOPROTEIN; HEMOGLOBIN; HYDROXAMIC ACID; MITOCHONDRIAL ENZYME; OXIDOREDUCTASE; OXYGEN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; SIDEROPHORE; SUPEROXIDE;

ARTICLE; ELECTRON TRANSPORT; ESCHERICHIA COLI; MICHAELIS CONSTANT; NONHUMAN; PRIORITY JOURNAL;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; RHIZOBIUM; RHIZOBIUM LEGUMINOSARUM BV. VICIAE;

EID: 0030956012     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/00221287-143-5-1557     Document Type: Article

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