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Titolo:
H2O2-forming NADH oxidase with diaphorase (cytochrome) activity from Archaeoglobus fulgidus
Autore:
Reed, DW; Millstein, J; Hartzell, PL;
Indirizzi:
Univ Idaho, Dept Microbiol Mol Biol & Biochem, Moscow, ID 83844 USA Univ Idaho Moscow ID USA 83844 l Mol Biol & Biochem, Moscow, ID 83844 USA
Titolo Testata:
JOURNAL OF BACTERIOLOGY
fascicolo: 24, volume: 183, anno: 2001,
pagine: 7007 - 7016
SICI:
0021-9193(200112)183:24<7007:HNOWD(>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
D-LACTATE DEHYDROGENASE; ESCHERICHIA-COLI; VULGARIS HILDENBOROUGH; MEMBRANE-VESICLES; OXIDATIVE STRESS; PURIFICATION; PROTEIN; PEROXIDE; INVOLVEMENT; REDUCTASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
37
Recensione:
Indirizzi per estratti:
Indirizzo: Hartzell, PL Univ Idaho, Dept Microbiol, Moscow, ID 83844 USA Univ Idaho Moscow ID USA 83844 crobiol, Moscow, ID 83844 USA
Citazione:
D.W. Reed et al., "H2O2-forming NADH oxidase with diaphorase (cytochrome) activity from Archaeoglobus fulgidus", J BACT, 183(24), 2001, pp. 7007-7016

Abstract

An enzyme exhibiting NADH oxidase (diaphorase) activity was isolated from the hyperthermophilic sulfate-reducing anaerobe Archaeoglobus fulgidus. N-terminal sequence of the protein indicates that it is coded for by open reading frame AF0395 in the A.fulgidus genome. The gene AF0395 was cloned and its product was purified from Escherichia coli. Like the native NADH oxidase(NoxA2), the recombinant NoxA2 (rNoxA2) has an apparent molecular mass of 47 kDa, requires flavin adenine dinucleotide for activity, has NADH-specific activity, and is thermostable. Hydrogen peroxide is the product of bivalent oxygen reduction by rNoxA2 with NADH. The rNoxA2 is an oxidase with diaphorase activity in the presence of electron acceptors such as tetrazolium, and cytochrome c. During purification NoxA2 remains associated with the enzyme responsible for D-lactate oxidation, the D-lactate dehydrogenase (Dld),and the genes encoding NoxA2 and Dld are in the same transcription unit. Together these results suggest that NADH oxidase may be involved in electrontransfer reactions resulting in sulfate respiration.

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Documento generato il 04/12/20 alle ore 22:40:12