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The Respiratory Chain

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Principles of Bioenergetics

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Abstract

The mitochondrial electron transport respiratory chain of higher animals is described. The main principles of energy conservation in the form of electrochemical potential of hydrogen ions are presented. Structural and functional properties of NADH: quinone-oxidoreductase, quinol: cytochrome c-oxidoreductase, and cytochrome c oxidase (complexes I, II, and IV) are described in detail. Possible mechanisms of transmembrane translocation of hydrogen ions by these enzymes are discussed.

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Notes

  1. 1.

    It is important to note that it is the standard redox potentials (E 0 ′) that are given both in the text and in Fig. 4.3. The real values of redox potentials (E) in a cell can differ substantially from those E 0 ′ values because of the difference in concentrations of corresponding oxidized and reduced forms of the redox compounds involved.

  2. 2.

    In the case of enterobacteria, NDH-1 consists of 13 subunits—not because of the lack of one of the main polypeptides, but rather due to fusion of the genes of two subunits (nuoC and nuoD) into one elongated gene (nuoCD).

  3. 3.

    We note that this principle (i.e. the fact that the mitochondrial genome possesses only the genes of the most hydrophobic subunits) is characteristic also for other respiratory chain components. Transport of such hydrophobic polypeptides through the cytoplasm and across the outer mitochondrial membrane would be very difficult. That is probably why the corresponding genes were left in the mitochondrial genome instead of being transferred together with the vast majority of other mitochondrial protein genes into the nucleus. This seems to be a likely explanation of why this unique organelle has kept its own genome.

  4. 4.

    Complex I from Thermus thermophilus, when compared to other homologous proteins, contains an extra [4Fe–4S] cluster (N7). But this cofactor is not conservative. It seems not to participate in electron transfer from NADH to quinone.

  5. 5.

    The radical form Y• is considered to be formed from the Tyr-244 residue. Generation of such an unusual and extremely reactive radical is probably the reason for formation of the covalent bond between Tyr-244 and a nearby His-240. This covalent bond probably stabilizes the radical form, which helps to avoid destruction of the protein.

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Authors and Affiliations

  1. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Vorobyevy Gory 1, Bldg. 44, Moscow, Russia, 119991

    Vladimir P. Skulachev & Alexander V. Bogachev

  2. Faculty of Biology, Moscow State University, Leninskie Gory 1-12, Moscow, Russia, 119991

    Felix O. Kasparinsky

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  1. Vladimir P. Skulachev
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  2. Alexander V. Bogachev
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  3. Felix O. Kasparinsky
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Correspondence to Vladimir P. Skulachev .

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Skulachev, V.P., Bogachev, A.V., Kasparinsky, F.O. (2013). The Respiratory Chain . In: Principles of Bioenergetics. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-33430-6_4

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  • DOI: https://doi.org/10.1007/978-3-642-33430-6_4

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