Cell Language Theory, The: Connecting Mind And Matter

128 The Cell Language Theory: Connecting Mind and Matter

b2861 The Cell Language Theory: Connecting Mind and Matter “6x9”

processes in the cell, including muscle contraction, movements of molec-

ular motors, e.g., kinesin and dynein [208], along microtubules in the

cytosol of the cell, and DNA supercoiling that accompany gene expres-

sion in the nucleus [79, 80] which do not involve any biomembranes and

hence is beyond the domain of application of the chemiosmotic model.

R. J. P. Williams (1926–2015) is another critic of the chemiosmotic

coupling concept. His criticism, aired from the very beginning of the che-

miosmotic conception, is based on the consideration of thermodynamic

efficiency [176, 209] which may still be valid. Below I list more specific

criticisms on the chemiosmotic hypothesis:

(1) Mitchell’s proposed mechanism for effectuating respiration-driven

proton translocation across the mitochondrial membranes is based on

what he calls vectorial metabolism or anisotropy of membrane pro-

tein organization [138, 139]. This idea seems to me to be insufficient

to account for oxidative phosphorylation, because structural organi-

zation alone, no matter how asymmetric, cannot give rise to asym-

metric distribution of the products of chemical reactions without

dissipating the requisite free energy. Without enzymologically realis-

tic mechanisms, the coupling between a down-hill (or exergonic)

reaction (e.g., oxidation of NADH to NAD+) and an up-hill (or ender-

gonic) chemical reaction or physical process (e.g., vectorial move-

ment of protons and asymmetric removal of water or the hydroxyl

group from the ATP synthesis center) would be prohibited by the

laws of thermodynamics. E. C. Slater (1817–2016) raised a similar

objection in [210]. To cause a symmetry breaking in molecular pro-

cesses without dissipating requisite free energy would violate the first

law of thermodynamics, e.g., because the resulting gradients could be

harnessed to do work, which is tantamount to creating energy anew.

(2) The ATP synthesizing portion of the reversible ATPase (i.e., F 1 ) is not

embedded within the mitochondrial inner membrane as Mitchell

originally assumed (see Figure 3.32(a)) but located outside the mem-

brane phase (see Table 3.5, Figures 3.35 and 3.36) attached to the

proton pumping F 0 component in the M phase through a set of long

polypeptide chains, i.e., the g- and e-subunits [211, 212]. If the proton

flow through F 1 is the necessary condition for ATP synthesis, it would

be difficult to explain why F 1 is not located within the M phase.

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