Cell Language Theory, The: Connecting Mind And Matter

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

F 0 -subunit is proposed by Oster and Wang which is explained in detail in

the legend to Figures 3.36 [162, 163]. Essentially, identical mechanisms

were proposed by Junge et al. [212] and Nath [161] (see Figure 3.37].

The internal structure of the F 1 F 0 ̃ATP synthase in mitochondria is

shown in Figures 3.35 (upper right-hand corner) and 3.36 (the left panel).

The relative arrangement of the a and c subunits of the F 0 portion of the

F 1 F 0 –ATP synthase in E. coli is highlighted in the left panel in Figure 3.36.

The key features involved are: (i) the two mutually non-collinear half chan-

nels labeled a and b, (ii) the arginine Arg-210 and histidine His-245 located

in the a subunit, and (iii) the aspartic acid Asp-61 in each of the 12 c subu-

nits. The c subunit is a complete cylinder, while the a subunit is a part of a

cylinder coaxial with c and covering two subunits of c at any given time.

Nath et al. [214, 215] assume that the negatively charged Asp-61 (see

leading ASP-61) is protonated when entering the half-channel open to the

inter-membrane space and deprotonated when entering the half-channel

open to the matrix space (see trailing Asp-61). When both Asp-61 residues

are deprotonated, the system is at equilibrium due to the electrostatic sta-

bilization afforded by positively charged His-245 and Arg-210. The pro-

ton concentration in the inter-membrane space, H+in, is higher than the

proton concentration in the vicinity of the leading Asp-61 residue. This

concentration gradient drives the proton through the half-channel, causing

proton to bind the leading Asp-61 residue. The neutralization of leading

Asp-61 allows the positively charged His-245 to attract the deprotonated

trailing Asp-61, causing the inner cylinder to rotate (see the arrow labeled

rotation). This makes the leading Asp-61 move out of the a–c interface

and into the membrane and a new protonated Asp-61 enters the a–c inter-

face. The unidirectionality of the rotation is guaranteed by the large free

energy barrier to transport a deprotonated Asp-61 from the a–c interface

into the hydrophobic membrane phase. When a new protonated Asp-61

residue enters the a–c interface from the left, it loses its proton to the

matrix space through the half-channel open to it. The proposed mecha-

nism will translocate 12 protons across the mitochondrial innermembrane

per complete rotation of the c subunit cylinder, causing a 360° rotation of

the g-subunit and the 360° rotary propagation of the conformational states

of the b-subunit of F 1 leading to the production of three molecules of ATP

(see Figure 3.35).

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