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Titolo:
Flavohemoglobin hmp affords inducible protection for Escherichia coli respiration, catalyzed by cytochromes bo ' or bd, from nitric oxide
Autore:
Stevanin, TM; Ioannidis, N; Mills, CE; Kim, SO; Hughes, MN; Poole, RK;
Indirizzi:
Univ Sheffield, Krebs Inst Biomolec Res, Dept Mol Biol & Biotechnol, Sheffield S10 2TN, S Yorkshire, England Univ Sheffield Sheffield S Yorkshire England S10 2TN S Yorkshire, England Natl Ctr Sci Res Demokritos, Ag Paraskevi Attiki 15310, Greece Natl Ctr Sci Res Demokritos Ag Paraskevi Attiki Greece 15310 310, Greece Univ London Kings Coll, Dept Chem, London WC2R 2LS, England Univ London Kings Coll London England WC2R 2LS London WC2R 2LS, England
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 46, volume: 275, anno: 2000,
pagine: 35868 - 35875
SICI:
0021-9258(20001117)275:46<35868:FHAIPF>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
FLAVOHAEMOGLOBIN HMP; OXIDATIVE-STRESS; C-OXIDASE; OXYGEN-AFFINITY; IN-VIVO; BINDING; NO; INHIBITION; MECHANISM; GENE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
59
Recensione:
Indirizzi per estratti:
Indirizzo: Poole, RK Univ Sheffield, Krebs Inst Biomolec Res, Dept Mol Biol & Biotechnol, FirthCourt,Western Bank, Sheffield S10 2TN, S Yorkshire, England Univ Sheffield Firth Court,Western Bank Sheffield S Yorkshire England S10 2TN
Citazione:
T.M. Stevanin et al., "Flavohemoglobin hmp affords inducible protection for Escherichia coli respiration, catalyzed by cytochromes bo ' or bd, from nitric oxide", J BIOL CHEM, 275(46), 2000, pp. 35868-35875

Abstract

Respiration of Escherichia coli catalyzed either by cytochrome bo' or bd is sensitive to micromolar extracellular NO; extensive, transient inhibitionof respiration increases as dissolved oxygen tension in the medium decreases. At low oxygen concentrations (25-33 muM), the duration of inhibition ofrespiration by 9 muM NO is increased by mutation of either oxidase. Respiration of an hmp mutant defective in flavohemoglobin (Hmp) synthesis is extremely NO-sensitive (I-50 about 0.8 muM); conversely, cells pre-grown with sodium nitroprusside or overexpressing plasmid-borne hmp(+) are insensitive to 60 muM NO and have elevated levels of immunologically detectable Hmp. Purified Hmp consumes O-2, at a rate that,is instantaneously and extensively (>10-fold) stimulated by MO due to NO oxygenase activity but, in the absence of NO, limp does not contribute measurably to cell oxygen consumption. Cyanide binds to Hmp (K-d 3 muM). Concentrations of KCN (100 muM) that do notsignificantly inhibit cell respiration markedly suppress the protection ofrespiration from NO afforded by Hmp and abolish NO oxygenase activity of purified Hmp, The results demonstrate the role of limp in protecting respiration from NO stress and are discussed in relation to the energy metabolism off. coli in natural O-2-depleted environments.

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Documento generato il 03/04/20 alle ore 11:16:02