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A representation of the structure of the mitochondrial ATP synthase is presented in Figure 2 of this document. Notably, the c


Figure 2 INTERMEMBRANE SPACE н* н at ATP ADP MATRIX (a) Subunit composition of the FF, ATP synthase The F, static component
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Ans: The ATP synthase enzyme in the course of evolution has remained conserved which is beneficial in that its mechanism somewhat follows the same whether in mitochondria or chloroplast, but still there remain subtle differences in their structure.
The chloroplast f0 complex is composed of a,b & c subunits which represent a motor like structure whose rotation causes the catalytic part (the f1 complex) to rotate and this brings about the formation of ATP.
The f0 complex has 3 major sub-units a,b and c and the 'c' sub-unit has further subsections that depend on species to species. The ring from S. cerevisiae contains 10 subunits, the ring from I. tartaricus contains 11 subunits & the ring from spinach S. oleracea contains 14 subunits. The stoichiometry is important because it is directly related to the proton-to-ATP ratio and the proton-motive-force (p.m.f.) required for each proton to drive the enzyme and considering 100 % efficiency that each full rotation brings about 3 ATP molecules, so the more sub-units the more protons and less p.m.f it requires.

The mitochondrial f0 complex has 3 major sub-units a,b,c and the 'c' sub-unit has further subsections containing 8 sub-units (as shown in bovine mitochondria), d, f6 and the oligomycin sensitivity-conferring protein (OSCP). The mechanism is similar and that the protonation and deprotonation of specific residues bring about the rotation of these subsections that in turn rotates the f1 complex.

The reason behind these structural differences is not clearly explained but it must be somehow related to the functional differences of the organelles.

Note: For any queries feel free to refer to the comment section.

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