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Regulatory Mechanisms of Proton-Translocating FOF1-ATP Synthase

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Bioenergetics

Part of the book series: Results and Problems in Cell Differentiation ((RESULTS,volume 45))

Abstract

H+-FOF1-ATP synthase catalyzes synthesis of ATP from ADP and inorganic phosphate using the energy of transmembrane electrochemical potential difference of proton (\(\Delta\tilde{\mu}_{\text{H}^{+}}\)). The enzyme can also generate this potential difference by working as an ATP-driven proton pump. Several regulatory mechanisms are known to suppress the ATPase activity of FOF1:

  1. 1.

    Non-competitive inhibition by MgADP, a feature shared by FOF1 from bacteria, chloroplasts and mitochondria

  2. 2.

    Inhibition by subunit ε in chloroplast and bacterial enzyme

  3. 3.

    Inhibition upon oxidation of two cysteines in subunit γ in chloroplast FOF1

  4. 4.

    Inhibition by an additional regulatory protein (IF1) in mitochondrial enzyme

In this review we summarize the information available on these regulatory mechanisms and discuss possible interplay between them.

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Authors and Affiliations

  1. ATP System Project, Exploratory Research for Advanced Technology, Japan Science and Technology Corporation (JST), 5800-3 Nagatsuta, Midori-ku, 226-0026, Yokohama, Japan

    Boris A. Feniouk

  2. Chemical Resources Laboratory, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, 226-8503, Yokohama, Japan

    Boris A. Feniouk & Masasuke Yoshida

  3. ICORP ATP-Synthesis Regulation Project (Japanese Science and Technology Agency), National Museum of Emerging Science and Innovation, 2-41 Aomi, Koto-ku, 135-0064, Tokyo, Japan

    Masasuke Yoshida

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  1. Boris A. Feniouk
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  2. Masasuke Yoshida
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Correspondence to Boris A. Feniouk or Masasuke Yoshida .

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Günter Schäfer Harvey S. Penefsky

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Feniouk, B.A., Yoshida, M. (2007). Regulatory Mechanisms of Proton-Translocating FOF1-ATP Synthase. In: Schäfer, G., Penefsky, H.S. (eds) Bioenergetics. Results and Problems in Cell Differentiation, vol 45. Springer, Berlin, Heidelberg. https://doi.org/10.1007/400_2007_043

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