Regulatory mechanisms of proton-translocating F(O)F (1)-ATP synthase.

Masasuke Yoshida, Boris A Feniouk

Journal: Results and problems in cell differentiation 2008;45():279-308

PMID: 18026702

Abstract

H(+)-F(O)F(1)-ATP synthase catalyzes synthesis of ATP from ADP and inorganic phosphate using the energy of transmembrane electrochemical potential difference of proton (deltamu(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 F(O)F(1): 1. Non-competitive inhibition by MgADP, a feature shared by F(O)F(1) from bacteria, chloroplasts and mitochondria 2. Inhibition by subunit epsilon in chloroplast and bacterial enzyme 3. Inhibition upon oxidation of two cysteines in subunit gamma in chloroplast F(O)F(1) 4. Inhibition by an additional regulatory protein (IF(1)) in mitochondrial enzyme In this review we summarize the information available on these regulatory mechanisms and discuss possible interplay between them.

Address: Exploratory Research for Advanced Technology, Japan Science and Technology Corporation , 5800-3 Nagatsuta, Midori-ku, 226-0026, Yokohama, Japan. [email protected]

DOI: 10.1007/400_2007_043

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https://dx.doi.org/10.1007/400_2007_043

MeSH Terms: Adenosine Diphosphate, Adenosine Triphosphate, Bacterial Proton-Translocating ATPases, Biochemistry, Catalysis, Chloroplast Proton-Translocating ATPases, Chloroplasts, Cysteine, Mitochondria, Mitochondrial Proton-Translocating ATPases, Models, Biological, Models, Molecular, Proton-Motive Force, Protons, Thermodynamics