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Which is the correct link between conformation of the beta-subunit of the F1 component of the ATP synthase and ADP+P¡ or ATP? loose Binding Change Mechanism binding ATP ADP+P. ATP C repeat ADP + P, ATP ATP ADP +P, tight binding open ATP loose => binding ADP+Pj open => catalyzes ADP+P¡ into ATP O tight => releases ATP open => releases ADP+P¡ O O

Which is the correct link between conformation of the beta-subunit of the F1 component of the ATP synthase and ADP+P¡ or ATP? loose Binding Change Mechanism binding ATP ADP+P. ATP C repeat ADP + P, ATP ATP ADP +P, tight binding open ATP loose => binding ADP+Pj open => catalyzes ADP+P¡ into ATP O tight => releases ATP open => releases ADP+P¡ O O

Human Anatomy & Physiology (11th Edition)
Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:Elaine N. Marieb, Katja N. Hoehn
Chapter1: The Human Body: An Orientation
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# Binding Change Mechanism of ATP Synthase **Question:** Which is the correct link between conformation of the beta-subunit of the F₁ component of ATP synthase and ADP + Pᵢ or ATP? **Diagram Explanation:** The diagram describes the binding change mechanism within ATP synthase, focusing on the conformation changes of the beta-subunit. This is crucial for the synthesis of ATP from ADP and inorganic phosphate (Pᵢ). - **First Conformation:** - Labeled as "open," depicted with ADP + Pᵢ loosely bound. - **Second Conformation:** - Transitions to a state labeled "tight binding," indicating the catalysis of ADP + Pᵢ into ATP. - **Third Conformation:** - Alters to release ATP, resetting the binding site for another cycle. This cycle continuously repeats, facilitating ATP production. **Multiple Choice Options:** - ☐ loose => binding ADP + Pᵢ - ☐ open => catalyzes ADP + Pᵢ into ATP - ☐ tight => releases ATP - ☐ open => releases ADP + Pᵢ This mechanism illustrates the efficiency of ATP synthase in energy production, essential for cellular processes.
Transcribed Image Text:# Binding Change Mechanism of ATP Synthase **Question:** Which is the correct link between conformation of the beta-subunit of the F₁ component of ATP synthase and ADP + Pᵢ or ATP? **Diagram Explanation:** The diagram describes the binding change mechanism within ATP synthase, focusing on the conformation changes of the beta-subunit. This is crucial for the synthesis of ATP from ADP and inorganic phosphate (Pᵢ). - **First Conformation:** - Labeled as "open," depicted with ADP + Pᵢ loosely bound. - **Second Conformation:** - Transitions to a state labeled "tight binding," indicating the catalysis of ADP + Pᵢ into ATP. - **Third Conformation:** - Alters to release ATP, resetting the binding site for another cycle. This cycle continuously repeats, facilitating ATP production. **Multiple Choice Options:** - ☐ loose => binding ADP + Pᵢ - ☐ open => catalyzes ADP + Pᵢ into ATP - ☐ tight => releases ATP - ☐ open => releases ADP + Pᵢ This mechanism illustrates the efficiency of ATP synthase in energy production, essential for cellular processes.
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