Biology
5th Edition
ISBN: 9781260487947
Author: BROOKER
Publisher: MCG
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Chapter 7, Problem 2CQ
What causes the rotation of the γ subunit of ATP synthase? How does this rotation promote ATP synthesis?
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Chapter 7 Solutions
Biology
Ch. 7.2 - Core Skill: Connections Look ahead to Table 45.1....Ch. 7.2 - Which organic molecules donate a phosphate group...Ch. 7.2 - Prob. 2CSCh. 7.4 - Prob. 1CCCh. 7.5 - Explain the meaning of the name cytochrome...Ch. 7.6 - Prob. 1CCCh. 7.6 - Prob. 1CSCh. 7.6 - Prob. 1EQCh. 7.6 - CoreSKILL In the experiment of Figure 7.13, what...Ch. 7.6 - Prob. 3EQ
Ch. 7.7 - Prob. 1CCCh. 7 - Which of the following pathways occurs in the...Ch. 7 - Prob. 2TYCh. 7 - Prob. 3TYCh. 7 - Which organic molecule supplies a two-carbon group...Ch. 7 - The ability to diagnose tumors using...Ch. 7 - Prob. 6TYCh. 7 - Certain drugs, which are called ionophores, cause...Ch. 7 - Prob. 8TYCh. 7 - Prob. 9TYCh. 7 - Prob. 10TYCh. 7 - Prob. 1CQCh. 7 - What causes the rotation of the subunit of ATP...Ch. 7 - Core Concept: Energy and Matter How is glucose...Ch. 7 - Discuss the advantages and disadvantages of...Ch. 7 - Prob. 2COQ
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- ATP synthase is composed of two oligomeric proteins, F and F₁. What is the function and purpose of each protein complex?arrow_forwardAccording to Paul Boyer, the mechanism of ATP synthesis involves the rotation of the y subunit which in turn causes sequential conformation changes in the aß assemblies. Explain the steps of ATP synthesis according to this mechanism.arrow_forwardDescribe the conformational changes (including substrates that bind to the different conformations) that occur in the F1 domain of ATP Synthase that result from protons flowing through the Fo domain down their concentration gradient:arrow_forward
- What is the major activator (non-allosteric, direct-activator) of phosphorylase? How does this activator activate phosphorylase (type of regulation)?arrow_forwardHow many net ATP are produced from the complete oxidation of one molecule of 1,3-bisphosphoglycerate (1,3 BPG) in a neuron?arrow_forwardIf an ATP Synthase complex had 16 c-subunits in the c-ring, how many ATPs will be made from a single rotation?arrow_forward
- If actively respiring mitochondria are exposed to an inhibitor of ATP-ADP translocase, the electrontransport chain ceases to operate. Why?arrow_forwardArrange the sequence of events in Oxidative Phosphorylation. (1-5) As the H+ ions move through the ATP synthase it'll provide the power to make the ATP synthase to turn. As it turns, a phosphate group is added to an ADP, forming a proton gradient-energy as ATP. With the help of a channel protein called ATP synthase, these H* ions are transferred back to the matrix. The electrons are passed to another electron carrier called cytochrome C (cyt C), which carries the = electrons to enzyme complex IV. Here, the last batch of H* ions are pumped into the intermembrane space. Enzyme complexes I and Il then transport the electrons through ubiquinone (Q), a mobile electron carrier. Q is reduced to QH, in the process and delivers the electrons to enzyme complex III. As this happens, more H* ions are pumped into the intermembrane space. The NADH and FADH2 produced from the previous stages of cellular respiration bring electrons across the transport chain to initiate the oxidative phosphorylation.arrow_forwardDicyclohexylcarbodiimide (DCCD) is a reagent that reacts with Asp or Glu residues. Explain why the reaction of DCCD with the c subunits of F1F0-ATP ase blocks its ATP-synthesizing activity.arrow_forward
- Why are ATPases hydrolases? Aren’t they also transferases as they move the phosphate group onto the protein in the sodium/potassium pump?arrow_forwardV-class proton pumps run backward relative to the F-class ATP synthase. Consider the cartoon, which shows the conformations of the beta-subunits and ATPIADP + Pj of the F-class synthase. Which of the following associations between the conformation of the beta subunit and ATP/ADP + P¡ is correct for V- Binding Change Mechanism loose binding ADP+P ATP ATP class pumps? C repeat ADP + P, ADP АТР tight binding АТР +P оpen АТР O The open conformation releases ATP. Hydrolysis of ATP to ADP + P¡ drives the change from tight to loose. O Binding of ADP + P¡ drives change from open to loose. Hydrolysis of ATP to ADP + Pj drives the change from open to loose.arrow_forwardWhy might a general ATP-binding inhibitor be a bad idea? Was this a problem with the drug that was developed?arrow_forward
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