When pure reduced cytochrome c is added to carefully preparedmitochondria along with ADP, P, antimycin A, and oxygen, thecytochrome c becomes oxidized, and ATP is formed, with a P/oratio approaching 1.0.(a) Indicate the probable flow of electrons in this system.(b) Why was antimycin A added?(c) What does this experiment tell you about the location of cou-pling sites for oxidative phosphorylation?(d) Write a balanced equation for the overall reaction (including cytc oxidation and ATP synthesis).

Cytochrome c is a hemeprotein and is a vital component of electron transport chain. The transfer of…

Answered: When pure reduced cytochrome c is added…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Citrate and isocitrate are interconverted via the enzyme aconitase: The standard free energy change for this reaction is +6.7 kJ/mol. In my pet llama's mitochondria, the free energy change was measured to be +0.8 kJ/mol. (No llamas were harmed in this experiment!) a. Calculate the [isocitrate]/[citrate] ratio in these mitochondria. b. If [isocitrate] =0.03 mM, what is [citrate]?
What compounds are the immediate source of the "high energy electrons" that enter the electron transport system of mitochondria? Where do these electron-donating compounds gain their electrons? What type of compounds are these electron-donating compounds?
Calculate how many moles of ATP can be made in standard conditions when 1 mole of protons flow back into the mitochondrial matrix through the ATP synthase. Assume that: i) the matrix pH is 7.8, ii) the cytosolic pH is 7.2, iii)ΔE=0.168 V (inside negative), iv) T=37°C, and v) the standard free energy change for the hydrolysis of 1 mole of ATP is -31.3 kJ/mol.
Under standard conditions, is the oxidation of free FADH2 by ubiquinone sufficiently exergonic to drive the synthesis of ATP? (F = 96.5 kJ/V • mol) ubiquinone + 2H++ 2e¯ → ubiquinol E' = 0.045 V FAD + 2H++ 2e → FADH2 = E' -0.219 V ○ no, as oxidation of FADH2 by ubiquinone generates 33.6 kJ/mol ○ no, as oxidation of FADH2 by ubiquinone generates 50.9 kJ/mol ○ no, as oxidation of FADH2 by ubiquinone generates -25.5 kJ/mol ○ yes, as oxidation of FADH2 by ubiquinone generates -33.6 kJ/mol ○ yes, as oxidation of FADH2 by ubiquinone generates -50.9 kJ/mol
Focusing on the mechanism linking complex I and ATP synthase depicted in figure 3 in the article, compare that hypothetical mechanism to the classical presentation described in our textbook. What are the major differences between this mechanism and Peter Mitchel’s original chemiosmotic theory? What are the similarities.
Which of the following is NOT true of Complex 1? a.) it's a proton pump and it pumps 4H+ into the intermembrane space for every pair of electrons donated by NADH. b.) electrons from NADH are accepted by an FMN prosthetic group within Complex I. c.) electrons from NADH are passed through Complex 1 prosthetic groups to ubiquinone. d.) it accepts electrons from either NADH or FADH2
How does DCPIP act as an indicator of presence of mitochondria? Will mitochondria in the presence of DCPIP still make ATP? Why or why not?
The following plot (percent of O2 bound versus [02]) shows three possible curves (A, B, C). In this case, "B" represents the normal oxygen transport protein. Suppose the local concentration of H+ increases. How might this be represented on the graph? Percent O₂ bound A OA shift from B to C B [0₂] OH+ concentration has no effect (remains curve B) OA shift from B to A
FAD is a coenzyme for dehydrogenation.(a) When a molecule is dehydrogenated, is FAD oxidizedor reduced?(b) Is FAD an oxidizing agent or a reducing agent?(c) What type of substrate is FAD associated with, and whatis the type of product molecule after dehydrogenation?(d) What is the form of FAD after dehydrogenation?(e) Use the curved-arrow symbolism to write a generalequation for a reaction involving FAD.
Rat heart muscle operating aerobically fills more than 90% of its ATP needs by oxidative phosphorylation. If each gram of tissue consumes O2 at the rate of 12.0 micromol/min, with glucose as the fuel source. (a) Calculate the rate at which the heart muscle consumes glucose and produces ATP. (b) Consider an alternate scenario – what would be the rate of consumption if the energy source was a solely triglycerides whose fatty acyl chains were each 14-C in length and saturated? (Assume the O2 consumption rate remains at 12.0 micromol/min) (c) For a steady-state concentration of ATP of 6.0 micromol/g of heart muscle tissue, calculate the time required (in seconds) to completely turn over the cellular pool of ATP if glucose us used as the sole fuel source. What does this result indicate about the need for tight regulation of ATP production? (Note: Concentrations are expressed as micromoles per gram of muscle tissue because the tissue is mostly water.)
When the antibiotic X is added to actively respiring mitochondria, several things happen: the yield of ATP decreases, the rate of O2 consumption increases, heat is released, and the pH gradient across the inner mitochondrial membrane increases. Does X act as an uncoupler or an inhibitor of oxidative phosphorylation? Explain the experimental observations in terms of the antibiotic’s ability to transfer K+ ions across the inner mitochondrial membrane.
The reduction potentials of iron in each of the cytochromes in the electron transport complexesvary from 0.The reduction potentials of iron in each of the cytochromes in the electron transport complexes vary from 0.1 V to 0.39 V. Explain why these different values are necessary for the operation of this process

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