Biochemistry (Looseleaf)
9th Edition
ISBN: 9781319114800
Author: BERG
Publisher: MAC HIGHER
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Question
Chapter 18, Problem 24P
Interpretation Introduction
Interpretation:
The reconciliation of discrepancy between requirements and resources.
Concept introduction:
ATP (adenosine triphosphate) is the energy source in the human body. It is formed in mitochondria, due to this mitochondria is 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.
Life requires energy. Describe the basic principles of bioenergetics in an animal cell. How is the flow and transformation of energy different in a photosynthesizing cell? Include the role of ATP and enzymes in your discussion.
The last stop. The final electron acceptor for the electron-transport
chain is which of the following? do
a. 0202
b. Coenzyme Q
с. СО2СО,
d. NAD+NAD+
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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- Chemiosmosis. ATP synthesis in chloroplasts is usually light dependent; it does not happen in the dark. When researchers shifted isolated chloroplasts from a low pH solution to a more alkaline (higher pH) solution, ATP synthesis occurred even in the absence of light! This was an experiment used to support the chemiosmosis mechanism of ATP formation in chloroplasts. Why? What would happen if the isolated chloroplasts were shifted to a lower pH solution? What would be the results if the above experiments were performed in the presence of light? If these experiments were performed in mitochondria instead of chloroplasts, what results would we expect?arrow_forwardFo-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.arrow_forwardFo-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 . The enzyme has 3 alpha-beta and 12 ‘c’ subunits. The mitochondrion maintains change in membrane potential=180 mV (negative inside), pHin = 8, pHout=7, [Pi] = 3 mM and ADP is present as well. . 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? full revolution of the crank (gamma subunit) produces 3 ATP.arrow_forward
- In full details. Define 'activation energy' of an enzyme catalysed single substrate reaction and mention the effects of an enzyme on this energy.arrow_forwardHigh potential. What is the equilibrium ratio of phosphoenolpyruvate to pyruvate under standard conditions when [ATP ]/[ ADP ]=10? [ATP]/[ADP] = 10?arrow_forwardAtp bookkeeping. Explain where the number of 38 and 32 atp per glucose molecules comes fromarrow_forward
- please help with this question. I am stuck. I listed the graph below ! Exergonic reactions such as the breakdown of ATP, are said to be “spontaneous.” However, by themselves, even exergonic reactions often proceed very slowly. What part of the curve helps to explain this?arrow_forwardSelect 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.arrow_forwardWorksheet. Draw the predicted graph of O, consumption and ATP synthesis for the following experiment: 1. Add ADP+Pi 2. Add succinate 3. Add rotenone 4. Add DNP 5. Add cyanidearrow_forward
- Help is appreciated. Think of an unusual eukaryotic species in which its ATP synthase has 12 subunits for its c ring. How many ATP molecules can be produced per pair of electrons that traverse the respiratory chian starting at Complex I? A. 2 ATP/2e- B. 1 ATP/2e- C. 0.5 ATP/2e- D. 1.5 ATP/2e- E. 3 ATP/2e-arrow_forwardReductive power. What ratio of NADPH to NADP+ is required to sustain [GSH] = 10 mM and [GSSG] = 1 mM ? Use the redox potentials given in Table 18.1 .arrow_forwardATP. Draw an ATP molecule and have an arrow pointing to the 'high-energy' bonds. See figure 6.13 for help.arrow_forward
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