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Titolo:
Purification of the 45 kDa, membrane bound NADH dehydrogenase of Escherichia coli (NDH-2) and analysis of its interaction with ubiquinone analogues
Autore:
Bjorklof, K; Zickermann, V; Finel, M;
Indirizzi:
Univ Helsinki, Dept Med Chem, Helsinki Bioenerget Grp, FIN-00014 Helsinki,Finland Univ Helsinki Helsinki Finland FIN-00014 Grp, FIN-00014 Helsinki,Finland
Titolo Testata:
FEBS LETTERS
fascicolo: 1, volume: 467, anno: 2000,
pagine: 105 - 110
SICI:
0014-5793(20000204)467:1<105:POT4KM>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
REFINED CRYSTAL-STRUCTURE; OXIDOREDUCTASE COMPLEX-I; LIPOAMIDE DEHYDROGENASE; RESOLUTION;
Keywords:
deamino-NADHI; idebenone; NDH-2; NADH; quinone reductase; ubiquinone; NAD(P)H-(disulfide)-oxidoredeductase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
17
Recensione:
Indirizzi per estratti:
Indirizzo: Finel, M Univ Helsinki, Dept Med Chem, Helsinki Bioenerget Grp, POB 8,Siltavuorenpenger 10, FIN-00014 Helsinki, Finland Univ Helsinki POB 8,Siltavuorenpenger 10 Helsinki Finland FIN-00014
Citazione:
K. Bjorklof et al., "Purification of the 45 kDa, membrane bound NADH dehydrogenase of Escherichia coli (NDH-2) and analysis of its interaction with ubiquinone analogues", FEBS LETTER, 467(1), 2000, pp. 105-110

Abstract

The NADH:ubiquinone reductase (NDH-2) of Escherichia coli was expressed asa His-tagged protein, extracted from the membrane fraction using detergentand purified by chromatography. The His-tagged NDH-2 was highly active andcatalyzed NADH oxidation by ubiquinone-l at rates over two orders of magnitude higher than previously reported. The purified, His-tagged NDH-2, like native NDH-2, did not oxidize deamino-NADH. Steady-state kinetics were usedto analyze the enzyme's activity in the presence of different electron accepters. High V-max and low KM values were only found for hydrophobic ubiquinone analogues, particularly ubiquinone-2, These findings strongly support the notion that NDH-2. is a membrane bound enzyme, despite the absence of predicted transmembrane segments in its primary structure, The latter observation is in agreement with possible evolutionary relation between NDH-2 andwater-soluble enzymes such as dihydrolipoamide dehydrogenase. There is currently, no clear indication of how NDH-2 binds to biological membranes, (C)2000 Federation of European Biochemical Societies.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 22/09/20 alle ore 15:31:49