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

See similar textbooks

Similar questions

When pure reduced cytochrome c is added to carefully prepared mitochondria along with ADP, Pi, antimycin A, and oxygen, the cytochrome c becomes oxidized, and ATP is formed, with a P/O ratio 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 coupling sitesfor oxidative phosphorylation?(d) Write a balanced equation for the overall reaction (including cyt c oxidation and ATP synthesis).(e) Calculate ΔG°′ for the above reaction, using E′0 values from Table 14.1and a ΔG°′ value for ATP hydrolysis of -32.2 kJ/mol.
When pure reduced cytochrome c is added to carefully prepared mito- chondria along with ADP, P, antimycin A, and oxygen, the cytochrome c becomes oxidized, and ATP is formed, with a P/O ratio approaching 1. Why was antimycin A added, and what does this experiment tell you about the location of coupling sites?
Inhibitors of electron transport have been used to determine the order of electron carriers. What would be the expected redox states of cytochrome a, bi, and c when the following inhibitors are added to succinate-driven respiring mitochondria? (i) myxothiazol (ii) antimycin A (iii) rotenone
Discuss the relationship between redox potentials E0’ and the organization of the components of the electron transport chain. Be specific, i.e., use data/actual values to back up your discussion. a) What are the values of E0’ for all the components of the ETS? b)How are the E0’ related to ∆G values? c) How do the values of E0’ vary among the participants in the ETS relative to their position in the ETS?
Skeletal muscle can store energy in the form of phosphocreatine, which is able to regenerate ATP. In relation to this, answer all of the following: (Show all your work for each part) a) Use your knowledge of bioenergentics to show why this statement is true. b) What is K¢eq for the overall reaction? c) Drawbiochemicalstructuresfortheoverallreaction. d) If the steady-state concentrations of phosphocreatine and creatine in a myocyte (muscle cell) are 1 uM and 129 uM, respectively, what will be the ratio of [ATP]/[ADP], assuming the creatine kinase reaction is at equilibrium?
Image shows reaction for hydrogen ion transport from outside mitochondrion to inside mitochondrion. Part a) What is ∆G ̊ for hydrogen ion transport. Part b) Outside the mitochondria there is a pH of 6.4 and inside mitochondria, there is a pH of 7.4. Calculate Q and ∆G for the reaction shown in the image. Part c) How many hydrogen ions needed per one ATP?
Interested in studying ethanol fermentation, you prepare two solutions of yeast extract that contains the cytosolic contents of Saccharomyces cerevisiae. You add glucose to both extracts at time zero, but to one (in red) you also add inorganic phosphate (added in two batches). Using a gas sensor, you monitor the CO2 generated by the two solutions over time and obtain the following data: a. Why is more CO2 generated upon the addition of phosphate? b. You become worried that the flasks would burst open to the build up in gas pressure. What other molecules could you add to the extract to slow down CO2 generation even in the presence of glucose and Pi?
The inhibitor X prevents coenzyme Q (Q) from participating in electron transfer in the electrontransport chain.(a) Will the presence of X prevent electrons from N ADH from passing through the electron trans-port chain? Explain why or why not.(b) Compound Y is a non-physiological reducing agent capable of directly reducing cytochromec1 in Complex III. Would oxygen consumption resume upon the addition of compound Y tomitochondria inhibited by inhibitor X? Be sure to explain your answer.
Terminal electron acceptors in anaerobic respiration include all of the following except A) O nitrate (NO,). B) O sulfate (So,2). C) O iron (Fe). D) O ammonia (NH,)
Four electron carriers, a, b, c, and d, whose reduced and oxidized formscan be distinguished spectrophotometrically, are required for respirationin a bacterial electron transport system. In the presence of substrates andoxygen, three different inhibitors block respiration, yielding the patterns ofoxidation states shown below. What is the order of the carriers in the chainfrom substrates to O2, and where do the three inhibitors act?O and R indicate fully oxidized and fully reduced, respectively.
You experiementally apply the compund antimyctin, which inhinits the functioning of complex III, cytochrome reductase, from participating in redox reactions. You follow this with the addition of 6 molecules of FADH2. How many total ATP molecules can be created using the number of protons that were pumped?
An enzyme is found that catalyzes the reaction X ⇌ Y. Researchers find that the Km for the substrate X is 4 μM, and the kcat is 20 min−1.(a) In an experiment, [X] = 6 mM, and V0 = 480 nM min−1. What was the [Et] used in the experiment?(b) In another experiment, [Et] = 0.5 μM, and the measured V0 = 5 μM min−1. What was the [X] used in the experiment?(c) The compound Z is found to be a very strong competitive inhibitor of the enzyme, with an α of 10. In an experiment with the same [Et] as in (a), but a different [X], an amount of Z is added that reduces V0 to 240 nM min−1. What is the [X] in this experiment?(d) Based on the kinetic parameters given above, has this enzyme evolved to achieve catalytic perfection? Explain your answer briefly, using the kinetic parameter(s) that define catalytic perfection.

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781319114671

Author:

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

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781319114671

Author:

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

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781305961135

Author:

Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Fundamentals of General, Organic, and Biological …

Biochemistry

ISBN:

9780134015187

Author:

John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson

Publisher:

PEARSON

SEE MORE TEXTBOOKS