The inhibition of NADH oxidase by the lower homologs of coenzyme Q
作者： Giorgio Lenaz , Petronio Pasquali , Enrico Bertoli , Giovanna Parenti-Castelli , Karl Folkers
DOI: 10.1016/0003-9861(75)90335-5
关键词:
摘要: Abstract The Coenzyme Q homologs having short isoprenoid chains are much less efficient than the higher in restoring NADH oxidation pentane-extracted lyophilized beef heart mitochondria; they have however high activity for succinate oxidation. same pattern is observed pentane extracted submitochondrial particles ETP only if quinones added to detergent-treated membranes, showing that there a decreased accessibility of long chain comparison with lower homologs. In intact mitochondria and ETP, CoQ 3 inhibits while leaving unaffected; inhibition by not reversed serum albumin but 7 , particularly when membrane has been previously “opened” deoxycholate. may accept electrons from cyanide-inhibited allowing coupling at first phosphorylation site as shown quenching fluorescence atebrine. mechanism probably related its insufficient rate reoxidation following segment respiratory it reduced dehydrogenase.
elsevier.com
sci-hub.se 参考文章(22)
Archie L. Smith, [13] Preparation, properties, and conditions for assay of mitochondria: Slaughterhouse material, small-scale Methods in Enzymology. ,vol. 10, pp. 81- 86 ,(1967) , 10.1016/0076-6879(67)10016-5
Sidney Fleischer, Becca Fleischer, [70] Removal and binding of polar lipids in mitochondria and other membrane systems Methods in Enzymology. ,vol. 10, pp. 406- 433 ,(1967) , 10.1016/0076-6879(67)10073-6
Allan G. Gornall, Charles J. Bardawill, Maxima M. David, Determination of serum proteins by means of the biuret reaction. Journal of Biological Chemistry. ,vol. 177, pp. 751- 766 ,(1949) , 10.1016/S0021-9258(18)57021-6
Marc Hansen, Archie L. Smith, Studies on the mechanism of oxidative phosphorylation: VII. Preparation of a submitochondrial particle (ETPH) which is capable of fully coupled oxidative phosphorylation Biochimica et Biophysica Acta. ,vol. 81, pp. 214- 222 ,(1964) , 10.1016/0926-6569(64)90036-7
Gottfried Schatz, Efraim Racker, Partial Resolution of the Enzymes Catalyzing Oxidative Phosphorylation Journal of Biological Chemistry. ,vol. 241, pp. 1429- 1438 ,(1966) , 10.1016/S0021-9258(18)96791-8
A. Kröger, M. Klingenberg, Quinones and Nicotinamide Nucleotides Associated with Electron Transfer Vitamins and Hormones Series. ,vol. 28, pp. 533- 574 ,(1971) , 10.1016/S0083-6729(08)60910-3
Lars Ernster, In-Young Lee, Birgitta Norling, Barbro Persson, Studies with ubiquinone-depleted submitochondrial particles FEBS Letters. ,vol. 3, pp. 21- 26 ,(1969) , 10.1016/0014-5793(69)80086-4
Ludmila Szarkowska, The restoration of DPNH oxidase activity by coenzyme Q (ubiquinone) Archives of Biochemistry and Biophysics. ,vol. 113, pp. 519- 525 ,(1966) , 10.1016/0003-9861(66)90228-1
J. Brya̵, Z. Kaniuga, E.C. Slater, Studies on the mechanism of inhibition of the mitochondrial electron transport by antimycin. II. Antimycin as an allosteric inhibitor Biochimica et Biophysica Acta (BBA) - Bioenergetics. ,vol. 189, pp. 317- 326 ,(1969) , 10.1016/0005-2728(69)90162-5
M. Gutman, Edna B. Kearney, Thomas P. Singer, Control of succinate dehydrogenase in mitochondria. Biochemistry. ,vol. 10, pp. 4763- 4770 ,(1971) , 10.1021/BI00801A025