Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
expand_more
expand_more
format_list_bulleted
Question
Chapter 20, Problem 14P
Interpretation Introduction
To propose:
The path of electrons through the Q cycle of complex III.
Introduction:
Due to complex III, movement of electrons from coenzyme Q to cytochrome c is there. The coenzyme Q possesses the ability to carry electrons and protons whereas cytochrome c carries only one electron. The Q cycle is a name given to the movement of electron via complex III.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
The ΔG°′ for hydrolytically removing a phosphoryl group from ATP is about twice as large as the ΔG°′ for hydrolytically removing a phosphoryl group from AMP (−14 kJ · mol−1). Explain the discrepancy.
Refer to the reaction scheme of the GAPDH catalyzed formation of 1,3-BPG. In the reaction, the nucleophile in step (4) is an inorganic phosphate molecule. The enzyme active site is elaborately constructed so that inorganic phosphate, not water, acts as the nucleophile.
What advantage is gained by using inorganic phosphate, instead of water, as the nucleophile? Discuss in terms of the energy yield of glycolysis. No need to calculate the total net energy yield of glycolysis.
During the process of synthesizing palmitate (C16), an acyl ACP __________. For the sake of this question, don’t treat acetyl ACP or malonyl ACP as an acyl ACP; assume the acyl ACP is a product at least 4 carbons long.
Choose ALL that apply.
(A) can be condensed with malonyl ACP to produce a Cn+2 b-ketoacyl ACP (B) is formed from the reduction of a trans D2-enoyl ACP(C) is a product of acetyl transacylase(D) is reduced by NADPH
(E) is a substrate for b-ketoacyl synthase(F) can be condensed with acetyl ACP to produce a Cn+2 b-ketoacyl ACP
Knowledge Booster
Similar questions
- Considering PNPP → PNP reaction, would you expect to see more intense or pale color for the reaction that contain the inhibitor? Explain.arrow_forwardMake an electron-flow-mechanism for this synthetic scheme. This involves predicting major and by-products using electronic and structural effects. The arrow push mechanism must be shown.(from the reaction of α-ketoacids and oxaprolines to proteins that contain native serine residues ) with labelarrow_forwardSuppose the biochemical pathway represented in Equation 5-10a is coupled at its first step to the hydrolysis of ATP to ADP. How would this change the expres- sion for AG of the pathway?arrow_forward
- Below are the reduction reactions for oxygen and FAD. ½202 + 2e + 2H+ → H20 E°' = 0.83 V FAD + 2e + 2H* → FADH2 E" = -0.22 V What is the potential (E") for the oxidation of FADH by oxygen? What is the AG®' for the oxidation of FADH, by oxygen? If we assume that the pumping of protons in conjunction with the oxidation of FADH, requires 120 kJ, what percentage of the energy from FADH oxidation is stored in the proton gradient (think about how many protons are pumped when FADH, transfers electrons to oxygen)?arrow_forwardComponents of ETC involved in redox reactions are organised from high energy to low energy”. Explain this statement and how does this play a role in transfer of electrons in ETC?arrow_forwardThe reaction in which glucose 6-phosphate (G6P) is converted to fructose 6-phosphate (F6P) is an example of an isomerization reaction. Notice that both molecules have the molecular formula C6H13O9P. The isomerization is catalyzed by glucose 6-phosphate isomerase. This is a reversible reaction in cells, with a moderately negative ΔG, but a very high activation energy. If you have a flask that contains a solution containing cellular concentrations of G6P and F6P, but no enzyme, how will the concentration of each molecule change over time?arrow_forward
- 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/molarrow_forwardLithium ion inhibits the synthesis of inositol trisphosphate by inhibiting a reaction in the breakdown of inositol trisphosphate.Explain this apparent paradox.arrow_forwardLithium ion inhibits the synthesis of inositol trisphosphate by inhibiting a reaction in the breakdown of inositol trisphosphate. Explain this apparent paradox.arrow_forward
- Explain why the coupled reaction ATP → ADP + Pi in the P-class ion pump mechanism does not involve direct hydrolysis of the phosphoanhydride bond.arrow_forwardBased on the definition of kcat, substitute a value that can be measured and yet still represents the value associated with the original concentration of the R. What would the rate or velocity of the reaction be equal to under these circumstances? How can cells increase Vmax? What variable that we could change would directly impact Vmax? Would the value of KM be affected by the ways you determined that Vma,x could be increased? What does this indicate about KM? Thinking about how catalysts work, about the Michaelis-Menten Equation, and the definition of kcat, what specifically does the enzyme change in the reaction mechanism to increase the rate? If an enzyme follows the 2 step mechanism proposed by Michaelis-Menten, what do you know about this enzyme? Be very specific and comprehensive. Please answer very soon will give rating surelyarrow_forwardIf a reaction has a ΔG°′ value of at least −30.5 kJ · mol−1, suffi -cient to drive the synthesis of ATP (ΔG°′ = 30.5 kJ · mol−1), can it still drive the synthesis of ATP in vivo when its ΔG is only −10 kJ · mol−1? Explain.arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning