The Bhopalator 65“6x9” b2861 The Cell Language Theory: Connecting Mind and Matteras structural elements. Therefore, it was inferred in 1972, in analogy to the
ETCs, that there exist proteins in the inner membrane of mitochondria that
mediate proton-transfer processes to accompany electrons and such proteins
were named the PTCs or “transprotonases” (in analogy to transhydrogenase)
as depicted in Figures 3.4(a) and 3.4(b). Although we cannot rule out the
possibility that PTC may exist as an independent protein or a protein complex
just as ETCs or transhydrogenases, the current experimental evidence appear
to indicate that PTC may constitute either a subunit or a domain of both ETC
(see Figures 3.39 and 3.40) or F 0 F 1 –ATP synthase (see Figure 3.36) in
agreement with Figure 3.4.
The charge separation in the ETC (symbolized as a square with bound
electron donor SH 2 and electron acceptor C in Figure 3.5(a)) is thought to
cause the local electrical polarization in ETC which then induces electrical
polarization in the ATP synthase, as schematically depicted in state b in
Figure 3.5(a), in agreement with Nath’s local electric field, ∆y [161]. The
electrically polarized and hence conformationally strained or deformed
ATP synthase (symbolized as a circle with bound ADP and Pi in state b in
Figure 3.5(a)) subsequently depolarizes or relaxes, leading to (i) the reduc-
tion of C to CH 2 and (ii) the synthesis of ATP from ADP and Pi. These two
chemical processes, i.e., the oxidation of SH 2 and the phosphorylation of
ADP, are not independent processes but are coupled in normal mitochon-
dria, i.e., one cannot proceed without the other, thus accounting for the
phenomenon of the “respiratory control” (see Figure 3.7(a) and [129,
p. 552]). Figure 3.5(b), reproduced from [144], shows the potential energy
diagram reflecting the postulated transformations among the three forms
of potential energies — electrical (E), mechanical (M), and chemical (C).
The EMC energy transduction is also expected to be involved in ion
movement through ion channels in biological membranes, both active and
passive, most likely implicating ion pairs or salt bridges (e.g., the carboxy-
late anion and the protonated amino groups of lysine or arginine) as sche-
matically shown in Figure 3.6, which was actually found to be the case in
the F 0 portion of the F 0 F 1 –ATP synthase in the 1990s (see Figures 3.35, 3.36
and [118, 119, 159]). Please note that, during the transition from a to b in
Figure 3.6, the salt bridges between the upper and lower ion pairs (to be
called the horizontal ion pairs) are broken and a new salt bridge is
formed between the left ion pairs (to be called the vertical ion pair).
During the b to c transition, the left vertical slat bridge is broken and theb2861_Ch-03.indd 65 17-10-2017 11:46:11 AM