Question

The residues that interact at the interface of the γ-subunit and the α/β protomers of ATP synthase are overwhelmingly hydrophobic. Describe the relationship between these subunits and how they interact during ATP synthesis and explain the benefit of having this large degree of hydrophobicity. (Think of how hydrophobic substances you know of feel).

Answer 1

Atp syhthase is complex 5 use in ETC

Complex 5--F0 and F1 subcomplex

F0-- hydrophobic ,made 10 C unit ,proton channel ,spain inner mitochondrial membrane

F1-- made up 9 subunit

3 alpha,

3 beta--atp synthesising unit

Gamma--rotating unit

Delta,E

In oxidative phosphorylation

Oxidative phase--electron jump,release of free energy,pump H+ intermembrane space

Phosphorylation--create potential difference due to jumping of electron

1

H+ moves to mitochondrial matrix through f0 unit

1

Rotation of gamma unit and confirmation change of beta unit ADP convert into ATP

This is called chemiosmotic theory

Atp synthase have hydrophobic unit is F0 which is act as proton pump help movement of H+ from matrix to mitochondrial space and synthesis ATP