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Principles of Bioenergetics pp 159–193Cite as

\( \Updelta \bar{\mu }_{{{\text{H}}^{ + } }} \)-Driven Chemical Work

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Abstract

The use of proton-motive force for performing chemical work is described. The structure and biochemical properties of F o F 1-type ATP synthase as well as the mechanism of energy transduction by this enzyme are thoroughly discussed. Characteristic properties of V o V 1-type and E 1 E 2-type ATPases are briefly described. Some other types of \( \Updelta \bar{\mu }_{{{\text{H}}^{ + } }} \)-motive chemical reactions, such as pyrophosphate synthesis, NADPH formation, and reverse transport of reducing equivalents in the respiratory chain are also reviewed.

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Notes

  1. 1.

    Besides ATP synthases of F o F 1-type, ATP synthases (ATPases) of V o V 1- and E 1 E 2-types may be also found in living organisms. The last sections of this chapter deal with these enzymes.

  2. 2.

    The number of c-type subunits of F o factor will be discussed in more detail later.

  3. 3.

    It should be stressed that in reality all the nucleotide-binding sites are located in the area of α and β subunit contacts. But in order to simplify the description, we will attribute these sites to those subunits which possess more amino acid residues participating in the formation of the corresponding sites.

  4. 4.

    This is true for the bacterial type enzyme; in the case of the mitochondrial enzyme, the central stalk is composed of subunits γ, δ, and ε.

  5. 5.

    These data are in accordance with the experimentally measured H+/ATP stoichiometry for chloroplast H+-ATP synthase. In the case of plants, ADP is photophosphorylated on the external side of the thylakoid membrane. The ATP obtained is mainly utilized in the chloroplast stroma during the synthesis of glucose. No porters participate in this process, and the H+/ATP ratio was shown to be about four protons per ATP molecule.

  6. 6.

    Catalytic sites are located in subunits A.

  7. 7.

    Two peripheral stalks are found in the vacuolar V 0 V 1-type ATPase.

  8. 8.

    Besides the membrane-bound transhydrogenase, the cells may also have a soluble transhydrogenase that catalyzes hydride ion transfer from NADPH to NAD+ in an energy-independent fashion. We will not discuss this enzyme in this book.

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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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Correspondence to Vladimir P. Skulachev .

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Skulachev, V.P., Bogachev, A.V., Kasparinsky, F.O. (2013). \( \Updelta \bar{\mu }_{{{\text{H}}^{ + } }} \)-Driven Chemical Work. In: Principles of Bioenergetics. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-33430-6_7

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