Vzaimodeistvie ubisemikhinona s suktsinatdegidrogenazoǐ i tsitokhromnoǐ tsep'iu mitokhondriǐ.

Translated title of the contribution: Interaction of ubisemiquinone with succinate dehydrogenase and the cytochrome chain of mitochondria

I. V. Grigolava, A. A. Konstantinov, M. I. Ksenzenko, E. K. Ruuge, A. N. Tikhonov

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

The free radical EPR signals of ubisemiquinone in mitochondria and submitochondrial particles (SMP) were investigated. One of the signals observed under the conditions of the respiratory chain highly oxidized and characterized by an unusually short time of the spin-lattice relaxation has previously been termed as SQ-2. The intensity of SQ-2 in SMP strongly depends on pH, the maximal concentration of QH. is reached at about 8.5. The signal is absent in the succinate dehydrogenase-depleted SMP and is highly sensitive to specific inhibitors of succinate: CoQ-oxidoreductase, such as alpha-thenoyltrifluoroacetone and carboxin. In SMP SQ-2 disappears in the presence of low concentrations of ferricyanide, while in mitochondria this non-penetrating oxidant provokes the appearance of SQ-2. The data obtained suggest that SQ-2 belongs to a stable ubisemiquinone which forms a complex with a FeS center of succinate dehydrogenase, is localized at the M-side of the membrane, and is kinetically isolated from the cytochrome chain. Oxidation of the terminal segment of the respiratory chain of mitochondria and SMP reduced by succinate in the presence of antimycin, is in some cases accompanied by an appearance of a strong free radical EPR signal which is stable at 77K but disappears rapidly in the frozen samples at -30- -40 degrees C. It is suggested that the signal is generated by an antimycin-insensitive oxidation of QH2 to QH. via the branch of the respiratory chain comprised of the Rieske FeS-protein and cytochrome c1. The mechanisms of how the two-electron oxidation-reduction of CoQ is coupled with the one-electron transfer through the cytochromes and FeS centers in the respiratory chain are discussed.

Original languageRussian
Pages (from-to)1970-1982
Number of pages13
JournalBiokhimiya
Volume47
Issue number12
Publication statusPublished - Dec 1982
Externally publishedYes

Fingerprint

coenzyme Q10
Mitochondria
Succinate Dehydrogenase
Cytochromes
Succinic Acid
Free Radicals
Paramagnetic resonance
Carboxin
Thenoyltrifluoroacetone
Cytochromes c1
Oxidation
Spin-lattice relaxation
Electrons
Oxidants
Oxidoreductases
Membranes
Electron Transport

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Grigolava, I. V., Konstantinov, A. A., Ksenzenko, M. I., Ruuge, E. K., & Tikhonov, A. N. (1982). Vzaimodeistvie ubisemikhinona s suktsinatdegidrogenazoǐ i tsitokhromnoǐ tsep'iu mitokhondriǐ. Biokhimiya, 47(12), 1970-1982.

Vzaimodeistvie ubisemikhinona s suktsinatdegidrogenazoǐ i tsitokhromnoǐ tsep'iu mitokhondriǐ. / Grigolava, I. V.; Konstantinov, A. A.; Ksenzenko, M. I.; Ruuge, E. K.; Tikhonov, A. N.

In: Biokhimiya, Vol. 47, No. 12, 12.1982, p. 1970-1982.

Research output: Contribution to journalArticle

Grigolava, IV, Konstantinov, AA, Ksenzenko, MI, Ruuge, EK & Tikhonov, AN 1982, 'Vzaimodeistvie ubisemikhinona s suktsinatdegidrogenazoǐ i tsitokhromnoǐ tsep'iu mitokhondriǐ.', Biokhimiya, vol. 47, no. 12, pp. 1970-1982.
Grigolava IV, Konstantinov AA, Ksenzenko MI, Ruuge EK, Tikhonov AN. Vzaimodeistvie ubisemikhinona s suktsinatdegidrogenazoǐ i tsitokhromnoǐ tsep'iu mitokhondriǐ. Biokhimiya. 1982 Dec;47(12):1970-1982.
Grigolava, I. V. ; Konstantinov, A. A. ; Ksenzenko, M. I. ; Ruuge, E. K. ; Tikhonov, A. N. / Vzaimodeistvie ubisemikhinona s suktsinatdegidrogenazoǐ i tsitokhromnoǐ tsep'iu mitokhondriǐ. In: Biokhimiya. 1982 ; Vol. 47, No. 12. pp. 1970-1982.
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