Biochemistry (Looseleaf)
9th Edition
ISBN: 9781319114800
Author: BERG
Publisher: MAC HIGHER
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Question
Chapter 18, Problem 43P
Interpretation Introduction
Interpretation:
The mechanism by which Arg 210 assist proton flow.
Concept introduction:
ATP (adenosine triphosphate) is the energy source in the human body. It is formed in mitochondria, due to this, mitochondria are also termed as the powerhouse of the cells. ATP contains three highly energetic phosphate groups. When any kind of energy consuming activity is performed by the body, then these phosphate groups get hydrolyzed from ATP, yielding a large amount of energy.
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Describe the steps by which the F0 portion of the ATP synthase harnesses the proton-motive force to help synthesize ATP. What would you expect to observe if the proton gradient were reversed? Explain your answer.
Fo-F1 ATPase. The energy for ATP synthesis from ADP and Pi is provided by the downhill transport of protons through the rotary FoF1 ATP synthase (lecture 22). The enzyme has 3 a-b and 12 ‘c’ subunits. The mitochondrion maintains Df=180 mV (negative inside), pHin = 8, pHout=7, [Pi] = 3 mM and ADP is present as well.
How much energy is available (from the proton electrochemical gradient) for ATP synthesis under these conditions (in kJ/mol)?
What [ATP]/[ADP] ratio will be established at steady-state under these conditions?
What would be the [ATP]/[ADP] ratio if the enzyme had only 9 ‘c’ subunits? Remember that full revolution of the crank (gamma subunit) produces 3 ATP.
Select all that apply.
What is true about the conformational aspects of coupling?
O The proton gradient is involved in the release of bound ATP from the synthase as a result of conformational change.
O The conformational states interconvert as a result of proton flux through the synthase.
There are two sites for substrate on the synthase and two possible conformational states: open (0) and tight-binding (T).
Dinitrophenol binds to and inhibits ATP synthase conformational changes, thus inhibiting ATP synthesis.
The Fo portion of ATP synthase acts as a rotary motor.
Chapter 18 Solutions
Biochemistry (Looseleaf)
Ch. 18 - Prob. 1PCh. 18 - Prob. 2PCh. 18 - Prob. 3PCh. 18 - Prob. 4PCh. 18 - Prob. 5PCh. 18 - Prob. 6PCh. 18 - Prob. 7PCh. 18 - Prob. 8PCh. 18 - Prob. 9PCh. 18 - Prob. 10P
Ch. 18 - Prob. 11PCh. 18 - Prob. 12PCh. 18 - Prob. 13PCh. 18 - Prob. 14PCh. 18 - Prob. 15PCh. 18 - Prob. 16PCh. 18 - Prob. 17PCh. 18 - Prob. 18PCh. 18 - Prob. 19PCh. 18 - Prob. 20PCh. 18 - Prob. 21PCh. 18 - Prob. 22PCh. 18 - Prob. 23PCh. 18 - Prob. 24PCh. 18 - Prob. 25PCh. 18 - Prob. 26PCh. 18 - Prob. 27PCh. 18 - Prob. 28PCh. 18 - Prob. 29PCh. 18 - Prob. 30PCh. 18 - Prob. 31PCh. 18 - Prob. 32PCh. 18 - Prob. 33PCh. 18 - Prob. 34PCh. 18 - Prob. 35PCh. 18 - Prob. 36PCh. 18 - Prob. 37PCh. 18 - Prob. 38PCh. 18 - Prob. 39PCh. 18 - Prob. 40PCh. 18 - Prob. 41PCh. 18 - Prob. 42PCh. 18 - Prob. 43PCh. 18 - Prob. 44PCh. 18 - Prob. 45PCh. 18 - Prob. 46PCh. 18 - Prob. 47PCh. 18 - Prob. 48PCh. 18 - Prob. 49PCh. 18 - Prob. 50PCh. 18 - Prob. 51PCh. 18 - Prob. 52PCh. 18 - Prob. 53PCh. 18 - Prob. 54PCh. 18 - Prob. 55PCh. 18 - Prob. 56PCh. 18 - Prob. 57PCh. 18 - Prob. 58PCh. 18 - Prob. 59P
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