메뉴 건너뛰기




Volumn 318, Issue 4, 2004, Pages 987-991

Absence of NADH channeling in coupled reaction of mitochondrial malate dehydrogenase and complex I in alamethicin-permeabilized rat liver mitochondria

Author keywords

Alamethicin; Complex I; Malate dehydrogenase; Mitochondria permeabilization; Mitochondrial respiration; NADH:ubiquinone oxidoreductase; Substrate channeling

Indexed keywords

ALAMETHICIN; GLUTAMIC ACID; LACTATE DEHYDROGENASE; MALATE DEHYDROGENASE; MALIC ACID; PROTEIN DERIVATIVE; PYRUVIC ACID; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE);

EID: 2442599389     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.04.131     Document Type: Article
Times cited : (11)

References (15)
  • 1
    • 0040777075 scopus 로고    scopus 로고
    • Model of a quinary structure between Krebs TCA cycle enzymes: A model for the metabolon
    • Vélot C., Mixon M.B., Teige M., Srere P.A. Model of a quinary structure between Krebs TCA cycle enzymes: a model for the metabolon. Biochemistry. 36:1997;14271-14276
    • (1997) Biochemistry , vol.36 , pp. 14271-14276
    • Vélot, C.1    Mixon, M.B.2    Teige, M.3    Srere, P.A.4
  • 2
    • 0034141634 scopus 로고    scopus 로고
    • Preliminary evidence for the existence of specific functional assemblies between enzymes of the beta-oxidation pathway and the respiratory chain
    • Parker A., Engel P.C. Preliminary evidence for the existence of specific functional assemblies between enzymes of the beta-oxidation pathway and the respiratory chain. Biochem. J. 345:2000;429-435
    • (2000) Biochem. J. , vol.345 , pp. 429-435
    • Parker, A.1    Engel, P.C.2
  • 3
    • 0021223549 scopus 로고
    • Binding of the enzymes of fatty acid beta-oxidation and some related enzymes to pig heart inner mitochondrial membrane
    • Sumegi B., Srere P.A. Binding of the enzymes of fatty acid beta-oxidation and some related enzymes to pig heart inner mitochondrial membrane. J. Biol. Chem. 259:1984;8748-8752
    • (1984) J. Biol. Chem. , vol.259 , pp. 8748-8752
    • Sumegi, B.1    Srere, P.A.2
  • 4
    • 0021744544 scopus 로고
    • Complex I binds several mitochondrial NAD-coupled dehydrogenases
    • Sumegi B., Srere P.A. Complex I binds several mitochondrial NAD-coupled dehydrogenases. J. Biol. Chem. 259:1984;15040-15045
    • (1984) J. Biol. Chem. , vol.259 , pp. 15040-15045
    • Sumegi, B.1    Srere, P.A.2
  • 5
    • 0028674909 scopus 로고
    • Binding of malate dehydrogenase and NADH channeling to complex I
    • Ovadi J., Huang Y., Spivey H.O. Binding of malate dehydrogenase and NADH channeling to complex I. J. Mol. Recogn. 7:1994;265-272
    • (1994) J. Mol. Recogn. , vol.7 , pp. 265-272
    • Ovadi, J.1    Huang, Y.2    Spivey, H.O.3
  • 6
    • 0024468918 scopus 로고
    • Substrate channeling of NADH and binding of dehydrogenases to complex I
    • Fukushima T., Decker R.V., Anderson W.M., Spivey H.O. Substrate channeling of NADH and binding of dehydrogenases to complex I. J. Biol. Chem. 264:1989;16483-16488
    • (1989) J. Biol. Chem. , vol.264 , pp. 16483-16488
    • Fukushima, T.1    Decker, R.V.2    Anderson, W.M.3    Spivey, H.O.4
  • 8
    • 0022233869 scopus 로고
    • Organization of Krebs tricarboxylic acid cycle enzymes in mitochondria
    • Robinson J.B. Jr., Srere P.A. Organization of Krebs tricarboxylic acid cycle enzymes in mitochondria. J. Biol. Chem. 260:1985;10800-10805
    • (1985) J. Biol. Chem. , vol.260 , pp. 10800-10805
    • Robinson Jr., J.B.1    Srere, P.A.2
  • 9
    • 0023655550 scopus 로고
    • Interaction between NAD-dependent isocitrate dehydrogenase, alpha-ketoglutarate dehydrogenase complex, and NADH:ubiquinone oxidoreductase
    • Porpaczy Z., Sumegi B., Alkonyi I. Interaction between NAD-dependent isocitrate dehydrogenase, alpha-ketoglutarate dehydrogenase complex, and NADH:ubiquinone oxidoreductase. J. Biol. Chem. 262:1987;9509-9514
    • (1987) J. Biol. Chem. , vol.262 , pp. 9509-9514
    • Porpaczy, Z.1    Sumegi, B.2    Alkonyi, I.3
  • 11
    • 0035937792 scopus 로고    scopus 로고
    • Catalytic activity of NADH-ubiquinone oxidoreductase (complex I) in intact mitochondria. Evidence for the slow active/inactive transition
    • Grivennikova V.G., Kapustin A.N., Vinogradov A.D. Catalytic activity of NADH-ubiquinone oxidoreductase (complex I) in intact mitochondria. Evidence for the slow active/inactive transition. J. Biol. Chem. 276:2001;9038-9044
    • (2001) J. Biol. Chem. , vol.276 , pp. 9038-9044
    • Grivennikova, V.G.1    Kapustin, A.N.2    Vinogradov, A.D.3
  • 12
    • 0037328645 scopus 로고    scopus 로고
    • In situ assay of the intramitochondrial enzymes: Use of alamethicin for permeabilization of mitochondria
    • Gostimskaya I.S., Grivennikova V.G., Zharova T.V., Bakeeva L.E., Vinogradov A.D. In situ assay of the intramitochondrial enzymes: use of alamethicin for permeabilization of mitochondria. Anal. Biochem. 313:2003;46-52
    • (2003) Anal. Biochem. , vol.313 , pp. 46-52
    • Gostimskaya, I.S.1    Grivennikova, V.G.2    Zharova, T.V.3    Bakeeva, L.E.4    Vinogradov, A.D.5
  • 13
    • 77957010110 scopus 로고
    • Isolation of liver or kidney mitochondria
    • Johnson D., Lardy H. Isolation of liver or kidney mitochondria. Methods Enzymol. 10:1967;94-96
    • (1967) Methods Enzymol. , vol.10 , pp. 94-96
    • Johnson, D.1    Lardy, H.2
  • 14
    • 0344631518 scopus 로고    scopus 로고
    • Substrate channeling
    • Spivey H.O, Ovadi J. Substrate channeling. Methods. 19:1999;306-321
    • (1999) Methods , vol.19 , pp. 306-321
    • Spivey, H.O.1    Ovadi, J.2
  • 15
    • 0026698788 scopus 로고
    • Glutamate-malate metabolism in liver mitochondria. a model constructed on the basis of mitochondrial levels of enzymes, specificity, dissociation constants, and stoichiometry of hetero-enzyme complexes
    • Fahien L.A., Teller J.K. Glutamate-malate metabolism in liver mitochondria. A model constructed on the basis of mitochondrial levels of enzymes, specificity, dissociation constants, and stoichiometry of hetero-enzyme complexes. J. Biol. Chem. 267:1992;10411-10422
    • (1992) J. Biol. Chem. , vol.267 , pp. 10411-10422
    • Fahien, L.A.1    Teller, J.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.