The Iron−Sulfur Clusters 2 and Ubisemiquinone Radicals of NADH:Ubiquinone Oxidoreductase Are Involved in Energy Coupling in Submitochondrial Particles† (original) (raw)

ArticleJanuary 28, 1997

Biochemistry

Cite this: Biochemistry 1997, 36, 4

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Published January 28, 1997

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Copyright © 1997 American Chemical Society

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The behavior of ubisemiquinone radicals and the iron−sulfur clusters 2 of NADH:ubiquinone oxidoreductase (Complex I) in coupled and uncoupled submitochondrial particles (SMP), oxidizing either NADH or succinate under steady-state conditions, was studied. Multifrequency EPR spectra revealed that the two new g z lines of the clusters 2, only observed during coupled electron transfer under conditions where energy dissipation is rate-limiting [De Jong, A. M. Ph., Kotlyar, A. B., & Albracht, S. P. J. (1994) Biochim. Biophys. Acta 1186, 163−171], are the result of a spin−spin interaction of 2.8 mT. Investigation of the radical signals present in coupled SMP indicated that more than 90% of the radicals can be ascribed to two types of semiquinones which are bound to Complex I (QI-radicals) or ubiquinol:cytochrome c oxidoreductase (Complex III; QIII-radicals). The presence of QIII-radicals, but not that of QI-radicals, was completely abolished by uncoupler. Part of the QI-radicals weakly interact with the clusters 2 of Complex I. This uncoupler-sensitive interaction can amount to a splitting of the radical EPR signal of at most 1 mT, considerably weaker than the 2.8 mT splitting of the g z lines of the clusters 2. We propose that the 2.8 mT splitting of these g z lines results from an energy-induced spin−spin interaction between the two clusters 2 within the TYKY subunit of Complex I. The two clusters 2 show no interaction during electron transfer in uncoupled SMP or in fully-reduced anaerobic-coupled SMP. The results point to a direct role of the Fe-S clusters 2 and the QI-radicals in the mechanism of coupled electron transfer catalyzed by Complex I.

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Copyright © 1997 American Chemical Society

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Biochemistry

Cite this: Biochemistry 1997, 36, 4

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Published January 28, 1997

Copyright © 1997 American Chemical Society

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