Binding change mechanism of ATP SYNTHASE
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THE SYNTHESIS OF ATP THROUGH OXIDATIVE PHOSPHORYLATION involves a conformational change in the enzyme complex
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1) Chemiosmotic theory proposed by Peter Mitchell describes how ATP synthesis is coupled to respiration via an electrochemical proton gradient generated by electron transport complexes pumping protons across the inner mitochondrial membrane.
2) Boyer's binding change mechanism describes how ATP synthase uses the proton gradient to drive the sequential binding and conformational changes of its beta subunits to synthesize ATP.
3) Factors that regulate oxidative phosphorylation include inhibitors that block electron transport complexes or uncouple the proton gradient from ATP synthesis.
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2. Peter Mitchell proposed the chemiosmotic theory to explain how this proton gradient is used to drive ATP synthesis. As protons flow back into the matrix through ATP synthase, the energy from their downhill movement is used to phosphorylate ADP into ATP.
3. The chemiosmotic theory states that the electron transport chain pumps protons across the inner mitochondrial membrane, creating an electrochemical proton gradient. This proton motive force drives ATP synthesis by ATP synthase.
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ATP synthase is an enzyme that generates ATP from ADP and inorganic phosphate using energy from the proton gradient across the inner mitochondrial membrane. It consists of two main parts - F0, which forms a channel for protons to pass through, and F1, which contains the catalytic sites to synthesize ATP. The passage of protons through F0 powers the rotation of F1, which facilitates the formation of ATP from ADP and phosphate at three catalytic binding sites. The overall reaction catalyzed by ATP synthase couples proton translocation across the membrane to ATP synthesis, and is essential for energy production in cells.
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Binding change mechanism of ATP SYNTHASE
- 1. ARIFA AKBAR ALI ARIFA.P.P DEPARTMENTOF BIOCHEMISTRY MARKAZ ARTS& SCIENCECOLLEGE, ATHAVANAD
- 2. ARIFA AKBAR ALI Proton-Translocating ATP Synthase Is Driven by Conformational Changes
- 3. ARIFA AKBAR ALI The mechanism of ATP synthesis by proton-translocating ATP synthase can be conceptually broken down into three phases: 1. Translocation of protons carried out by F0. 2. Catalysis of formation of the phosphoanhydride bond of ATP carried out by F1. 3. Coupling of the dissipation of the proton gradient with ATP synthesis, which requires interaction of F1 and F0.
- 4. ARIFA AKBAR ALI F1 is proposed to have three interacting catalytic protomers, each in a different conformational state: one that binds substrates and products loosely (L state), one that binds them tightly (T state), and one that does not bind them at all (open or O state). The free energy released on proton translocation is harnessed to interconvert these three states. The phosphoanhydride bond of ATP is synthesized only in the T state and ATP is released only in the O state.
- 5. ARIFA AKBAR ALI 1. Binding of ADP and Pi to the “loose” (L) binding site. 2. A free energy–driven conformational change that converts the L site to a “tight” (T) binding site that catalyzes the formation of ATP. This step also involves conformational changes of the other two subunits that convert the ATP-containing T site to an “open” (O) site and convert the O site to an L site. The reaction involves three steps
- 6. ARIFA AKBAR ALI 3. ATP is synthesized at the T site on one subunit while ATP dissociates from the O site on another subunit. On the surface of the active site, the formation of ATP from ADP and Pi entails little free energy change, that is, the reaction is essentially at equilibrium. Consequently, the free energy supplied by the proton flow primarily facilitates the release of the newly synthesized ATP from the enzyme; that is, it drives the T & O transition, thereby disrupting the enzyme–ATP interactions that had previously promoted the spontaneous formation of ATP from ADP Pi in the T site.