The reason for, FAD is better electron acceptor than NAD+ in the reaction catalyzed by succinate dehydrogenase. Concept introduction: An electron transport chain (ETC) is the series of redox reactions that involves the transfer of electrons from electron donors to electron acceptors. This transfer of electrons is coupled with the proton transfer (H + ) across the membrane. This then creates the electrochemical gradient resulting in the formation of ATP.

Question

Want to see the full answer?

Answer 1

Question

Chapter 18, Problem 10P

Interpretation Introduction

Interpretation:

The reason for, FAD is better electron acceptor than NAD+ in the reaction catalyzed by succinate dehydrogenase.

Concept introduction:

An electron transport chain (ETC) is the series of redox reactions that involves the transfer of electrons from electron donors to electron acceptors. This transfer of electrons is coupled with the proton transfer (H⁺) across the membrane. This then creates the electrochemical gradient resulting in the formation of ATP.

Expert Solution & Answer

Want to see the full answer?

Check out a sample textbook solution

See solution

Students have asked these similar questions

Select 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.

. Pyruvate can be processed under anaerobic conditions to ethanol (in yeast) or to lactate (in mammals), as shown. Explain the primary purpose of these reactions. Describe the major biochemical features of each reaction

not true about the Michaelis-Menten equation? The equation that gives the rate, v, of an the substrate concentration [S] is the Michaelis-Menten equation = Vmax[S]/(Km + [S]), where V, enzyme-catalyzed reaction for all values of max and Km are constants. Which of the following is a) for [S] << Km, V = Vmax applies to most enzymes, but allosteric enzymes have different kinetics when [S] = Km, then v = Vmax/2 gives the rate when the enzyme concentration, temperature, pH, and ionic strength are constant for very high values of [S], v approaches Vmax e) Which is correct about the constant Km in the Michaelis-Menten equation? also called the catalytic constant or turnover number equal to the number of product molecules produced per unit time when the enzyme is saturated with substrate it is the constant in the first order rate equation v = k[A] it is the constant in the second order rate equation v = equal to the substrate concentration at which the velocity or rate of a reaction is ½ the…