Assay conditions for the mitochondrial NADH:coenzyme Q oxidoreductase
作者： Ernesto Estornell , Romana Fato , Francesco Pallotti , Giorgio Lenaz
DOI: 10.1016/0014-5793(93)80498-J
关键词:
摘要: The assay of Complex I activity requires the use artificial acceptors, such as short-chain coenzyme Q homologs and analogs, because physiological quinones, CoQ10, are too insoluble in water to be added substrates media. medical interest raised last years on pathological changes has focussed requirement easy reliable assays for its analysis. We have undertaken a systematic examination conditions mitochondrial membranes, using series quinones electron particularly CoQ0, CoQ1 CoQ2, analogs duroquinone decylubiquinone. Our findings pointed out that most suitable acceptor NADH:CoQ reductase is homolog CoQ1. analog DB, commercially available, although yielding high activity, nevertheless causes some problems standardization conditions.
elsevier.com
researchgate.net 
sci-hub.se 参考文章(19)
A. Lewis Farr, Oliver H. Lowry, Rose J. Randall, Nira J. Rosebrough, Protein Measurement with the Folin Phenol Reagent Journal of Biological Chemistry. ,vol. 193, pp. 265- 275 ,(1951)
Giorgio Lenaz, Petronio Pasquali, Enrico Bertoli, Giovanna Parenti-Castelli, Karl Folkers, The inhibition of NADH oxidase by the lower homologs of coenzyme Q Archives of Biochemistry and Biophysics. ,vol. 169, pp. 217- 226 ,(1975) , 10.1016/0003-9861(75)90335-5
Mauro Degli Esposti, Giorgio Lenaz, Kinetics of ubiquinol-1-cytochrome c reductase in bovine heart mitochondria and submitochondrial particles. Biochimica et Biophysica Acta. ,vol. 682, pp. 189- 200 ,(1982) , 10.1016/0005-2728(82)90098-6
Qin-Shi Zhu, Sallie G. Sprague, Diana S. Beattie, Reduction of exogenous quinones and 2,6-dichlorophenol indophenol in cytochrome b-deficient yeast mitochondria: a differential effect on center i and center o of the cytochrome b-c1 complex. Archives of Biochemistry and Biophysics. ,vol. 265, pp. 447- 453 ,(1988) , 10.1016/0003-9861(88)90148-8
Min Chen, Bel-Li Liu, Lian-quan Gu, Qin-shi Zhu, The effect of ring substituents on the mechanism of interaction of exogenous quinones with the mitochondrial respiratory chain. Biochimica et Biophysica Acta. ,vol. 851, pp. 469- 474 ,(1986) , 10.1016/0005-2728(86)90083-6
John E. Walker, The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains. Quarterly Reviews of Biophysics. ,vol. 25, pp. 253- 324 ,(1992) , 10.1017/S003358350000425X
Peter Mitchell, Protonmotive redox mechanism of the cytochrome b-c1 complex in the respiratory chain: protonmotive ubiquinone cycle. FEBS Letters. ,vol. 56, pp. 1- 6 ,(1975) , 10.1016/0014-5793(75)80098-6
C.Ian Ragan, NADH-ubiquinone oxidoreductase. Biochimica et Biophysica Acta. ,vol. 456, pp. 249- 290 ,(1976) , 10.1016/0304-4173(76)90001-X
Yieh-Ping Wan, Robert H. Williams, Karl Folkers, Kam Hung Leung, Efraim Racker, Low molecular weight analogs of coenzyme Q as hydrogen acceptors and donors in systems of the respiratory chain. Biochemical and Biophysical Research Communications. ,vol. 63, pp. 11- 15 ,(1975) , 10.1016/S0006-291X(75)80003-9
F.J. Ruzicka, F.L. Crane, Four quinone reduction sites in the NADH dehydrogenase complex Biochemical and Biophysical Research Communications. ,vol. 38, pp. 249- 254 ,(1970) , 10.1016/0006-291X(70)90704-7