Abstract
It is presently recognized that the transfer of electrons from substrates to molecular oxygen in mitochondria involves integral membrane protein complexes containing redox groups of increasing redox potentials (Tzagoloff, 1982). According to the original intuition of Green (1966), it is widely accepted that electron transfer between complexes is ensured by mobile components acting as cosubstrates, vz. ubiquinone (Q) and cytochrome c (cyt.c). In particular, ubiquinone holds a central position in the chain, being reduced by a large collection of flavoprotein dehydrogenases and reoxidized by the ubiquinol-cyt.c reductase complex (bql complex or Complex III)(Lenaz et al., 1985 b): such position is likely to mark a strategic point for a regulatory role in electron transfer.
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Lenaz, G. et al. (1988). Role of Ubiquinone Diffusion in Mitochondrial Electron Transfer. In: Lemasters, J.J., Hackenbrock, C.R., Thurman, R.G., Westerhoff, H.V. (eds) Integration of Mitochondrial Function. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-2551-0_4
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