Biochemistry
Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Chapter 21, Problem 15P
Interpretation Introduction

(a)

Interpretation:

The consequence of c-subunit stoichiometry for the ratio of hydrogen ion and ATP needs to be determined.

Concept Introduction:

The several types of ATP syntheses are A-type, F-typeand V-type. The main transmembrane subunit of these ATP syntheses is ATPase subunit C of Fo/Vo complex.

They are enzyme complexes which are membrane-bound, and they also transport ions like protons across the membrane. The energy can be produced in the form proton gradient making use of flux of the ions through the membrane with the help of ATPase proton network that drives the ATP synthesis.

Some of the ATPases use the energy obtained from ATP hydrolysis and build proton gradient. In this way, they work in reverse direction. The different ATPase types have different functions and the ion type transported by them.

Interpretation Introduction

(b)

Interpretation:

The relationship between c-subunit stoichiometry and the magnitude of the proton-motive force needs to be explained.

Concept Introduction:

For ATP synthesis, the approximate value of the proton motive force is -250 mV. This is denoted as Δp and composed of membrane potential, Δϕ and pH gradient ΔpH . The proton movie force is ratio of change in Gibbs free energy and Faraday’s constant. Thus, the formula will be as follows:

  Δp=ΔGθ=Δϕ(2.3RTθ)ΔpH

In the chloroplast the value of Δϕ is -50 to -100 mV. Also, the value of pH gradient is approximately 3 units. The value of photon motive force can be calculated from the above formula. It is approximately -170 mV.

The subunit C in F-ATPases is also known as subunit 9 as well as proteolipid. The F-ATPases contains 10 C subunits in the form of an oligomeric ring that build up the Fo rotor up.

The protons flux drives the C subunit ring rotation that is coupled with the F1 complex gamma subunit rotor. There is permanent bonding between the epsilon and gamma subunits in F1 and C subunit ring of Fo .

The continuous protonation and deprotonation of Asp61 in the subunit C results in the movement of the rotor stepwise.

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Enzymes normally enhance the rates of biochemical reactions by preferentially binding and stabilizing the transition states rather than either the substrates or the products of a reaction. The F|-subunit of ATP synthase does not fit this norm so well as tight binding to ATP rather than a transition state is employed to make ATP. Explain the binding-change model of the mechanism of ATP-synthase. How and why is the proton-motive force used in the reaction cycle of ATP synthase?
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