Biochemistry
Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
Question
Book Icon
Chapter 20, Problem 9P
Interpretation Introduction

(a)

To calculate:

The change of standard free energy for the given reaction.

Introduction:

Succinate dehydrogenase is also known as SQR succinate Q reductase is seen in the cells of bacteria as a complex enzyme. It is also found in the eukaryotes in the membrane of inner mitochondria. Thus enzyme takes part in the electron transport chain and citric acid cycle.

Expert Solution
Check Mark

Explanation of Solution

The electron acceptor is O2 and the electron donor is succinate which is determined from the half reactions:

  Fumarate+2H++2eSuccinate+(E0'=+0.031V)

  12O2+2H++2eH2O,(E0'=+0.816V)

The free change of energy for the reaction is calculated by determining the change of the standard potential:

  ΔE0'=acceptorΔE0'donorΔE0'

  =+0.816V(0.031V)=+0.785V

  ΔG0'=nFΔE0'n=2F=96,485kJ/Vmol

  =2(96.485kJ/V.mol)(0.785V)=151.5kJ/mol

Interpretation Introduction

(b)

To calculate:

The equilibrium constant of the reaction.

Introduction:

Succinate dehydrogenase is also known as SQR succinate Q reductase is seen in the cells of bacteria as a complex enzyme. It is also found in the eukaryotes in the membrane of inner mitochondria. Thus enzyme takes part in the electron transport chain and citric acid cycle.

Expert Solution
Check Mark

Explanation of Solution

  ΔG0'=RTlnKeqKeq=e ΔG RT

  =e (151.5) (8.314× 10 3 )(298)=3.60×1026

Interpretation Introduction

(c)

To determine:

The release of the actual free energy accompanying the coenzyme Q reductase of NADH is equal to releasing amount under the normal condition

Introduction:

Succinate dehydrogenase is also known as SQR succinate Q reductase is seen in the cells of bacteria as a complex enzyme. It is also found in the eukaryotes in the membrane of inner mitochondria. Thus enzyme takes part in the electron transport chain and citric acid cycle.

Expert Solution
Check Mark

Explanation of Solution

From the given we have,

  G=151.3kJ/mol for 2 ATP

So with 70% efficiency,

  151.3kJ/mol×0.70=106.1kJ/mol

For 1 ATP,

  53.1kJ/mol

With the equation,

  ΔG=ΔG0+RTln(ATP)(ADP)(Pi)

  (ATP)(ADP)=(Pi)×eΔGΔG 0'RT

  =(1mM)×e (53.0530.5) (8.314× 10 3 )(298)=8.89

The ratio of ATP and ADP maximum for the phosphorylation oxidative occurring at Pi =1 mM is 8.89.

Want to see more full solutions like this?

Subscribe now to access step-by-step solutions to millions of textbook problems written by subject matter experts!
Students have asked these similar questions
Referring to for E′0 values, calculate ΔG°′ for oxidation of malate by malate dehydrogenase.
Given the following information, calculate the physiological ΔG of the isocitrate dehydrogenase reaction at 25°C and pH 7.0: [NAD+]/[NADH] = 8, [α-ketoglutarate] = 0.1 mM, and [isocitrate] = 0.02 mM. Assume standard conditions for CO2 (ΔG°′ is given in Table). Is this reaction a likely site for metabolic control?
[AktivGrid] Draw the product of the reaction of isocitrate catalyzed by isocitrate dehydrogenase in the TCA (citric acid) cycle. Provide the structure in the protonation state found in physiological conditions. rxn' F-C-H NAD+ isocitra te dehydro genase NADH, Dra H+, > Problem 5 of 12 Submit H Atoms, Bonds and Rings OH Charges CH2OH Drag To Pan CH2OH- H OH Undo Reset ―CH2OH- Remove Done ⚫SH CHO +
Knowledge Booster
Background pattern image
Similar questions
SEE MORE QUESTIONS
Recommended textbooks for you
  • Text book image
    Biochemistry
    Biochemistry
    ISBN:9781305577206
    Author:Reginald H. Garrett, Charles M. Grisham
    Publisher:Cengage Learning
Text book image
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning