The Bhopalator 125“6x9” b2861 The Cell Language Theory: Connecting Mind and Mattersynthase do not participate in the chemistry of ATP synthesis in F 1 (as
claimed in Figure 3.32(b)), but these two processes, i.e., the proton flow
through F 0 and ATP synthesis in F 1 , are coupled through the g-subunit that
transmits the torsional (also called mechanical or conformational) strains
(i.e., conformons discussed in Section 3.4) generated by the proton-driven
rotary motions of F 0 to the rotary propagation of the conformational waves
in the a 3 b 3 portion of F 1 which catalyzes the phosphorylation of ADP and
de-binding of ATP (see Figure 3.36).
The quantitative aspect of the chemiosmotic model summarized as
Feature (5) seems largely invalidated, as well since (i) the H+/2e- stoichi-
ometry is about 4 for coupling sites 1, 2, and 3 [118, 162, 177] and not 2
and (ii) H+/ATP stoichiometry is 8/3 = 2.7 in animals and 10/3 = 3.33 in
yeast [240] and not 2. In other words, according to the chemiosmotic
model, these two stoichiometries must be equal, H+/2e- = H+/ATP, but in
fact they are not, which agree with the conformon model of oxphos,
according to which the H+/2e- = n depends on the relative rates of step 2
(intramembrane proton transfer) and step 3 (trans-membrane proton trans-
fer) (see Figure 3.29), while H+/3ATP = m is fixed by the number of pro-
ton binding sites on the F 0 component of F 1 F 0 –ATP synthase whichFigure 3.33 The F 1 F 0 -ATP synthase on the plasma membranes of tumor, endothelial, and
liver cells. Reproduced from [207].b2861_Ch-03.indd 125 17-10-2017 11:46:43 AM