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H+-ATPase as an Energy-Converting Enzyme

Hamamoto, Toshiro ; Kagawa, Yasuo

The Enzymes of Biological Membranes, p.149-176

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Título:
H+-ATPase as an Energy-Converting Enzyme
Autor: Hamamoto, Toshiro ; Kagawa, Yasuo
Assuntos: Adenosine Triphosphatase ; Beef Heart ; Catalytic Site ; Coupling Factor ; Thermophilic Bacterium
É parte de: The Enzymes of Biological Membranes, p.149-176
Descrição: The main energy sources of living organisms are oxidative and photosynthetic phosphorylation. In both reactions, the energy is finally transduced to the chemical bond energy of ATP by H+-ATPase (EC 3.1.6.3). A part of H+-ATPase was first demonstrated in mitochondria as coupling factor 1 which hydrolyzed ATP and recovered the oxidative phosphorylation of submitochondrial particles depleted of their coupling factor 1 (Penefsky et al., 1960). The role of H+-ATPase has been understood in the light of the chemiosmotic theory; an electrochemical potential difference across the membrane is formed by respiration or photoreduction and H+-ATPase synthesizes ATP from ADP and Pi consuming the energy of H+ flow (Mitchell, 1979; Ferguson and Sorgato, 1982).
Editor: Boston, MA: Springer US
Idioma: Inglês

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