Electrons consilient mechanism

Thus, the challenge to the consilient mechanisms posed by the electron transport chain transforms into a showcase example that includes the two distinct but interlinked physical processes of the development of entropic elastic force during hydrophobic association to bring both consilient mechanisms to bear. 

Relevance of the Consilient Mechanisms to the Coupling of Electron Transport to Proton Gating/Pumping... 

Consilient Mechanisms for Electron Transfer/Proton Transport Reside in the Movement of the Rieske Iron Protein FeS Center... 

The focus has been on both aspects of the consilient mechanism (hydrophobic association/ dissociation and elastic force development/ relaxation) involved in the unique domain movement for electron transfer within Complex III. In what follows, the same aspect of hydrophobic association/dissociation of the consilient mechanism is proposed for facilitating proton gating. 

Our conclusion is that dissociation of the RIP from the Q site in a single step represents a unique intersection of electron transfer and proton translocation that simultaneously employs both the hydrophobic and elastic consilient mechanisms. 

Crystal structure data on Complex IV developed relatively early - compared with the other complexes of the electron transport chain. Nonetheless, the understanding of mechanism does not rise to the same level, for example, as that of Complex III. The following consideration of Complex IV is less extensive than that for Complex III above, but it continues to argue for the hydrophobic consilient mechanism by means of the apolar-polar repulsive free energy of hydration, AG,p, and it also speculates on possible molecular players for proton egress and ingress. 

In relation to the hydrophobic consilient mechanism, it is relevant to note that the redox centers are positively charged metal ions that become less charged on the addition of the electron and more charged on oxidation. In general, the effect of reduction of the redox sites, for example, heme iron and copper centers, is to increase hydrophobicity. Because a change in the redox state results in proton translocation, the protein-based machine. Complex IV, performs electro-chemical transduction. 

The concept of two distinct but interlinked mechanical processes, expanded here as the coupling of hydrophobic and elastic consilient mechanisms, entered the public domain in the publication of Urry and Parker. Experimental results on elastic-contractile model proteins forged the concept, and the work of Urry and Parker extended the concept to contraction in biology. Unexpected in our examination of the relevance of this perspective to biology was to find the first clear demonstration of the concept in biology in a protein-based machine of the electron transport chain as a transmembrane protein of the inner mitochondrial membrane. Unimaginable was the occurrence of the coupled forces precisely at the nexus at which electron transfer couples to proton pumping. 

We have discussed the nexus of hydrophobic and elastic consilient mechanisms in Complex III at the intersection of electron flow and proton translocation (electro-chemical transduction) that was unimaginable, absent the detailed analysis of structure. The hydrophobic and elastic consilient mechanisms, however, when applied to the general structure and phenomenology of the Fi-motor of ATP synthase (chemo-chemical transduction), gave rise to a host of successful predictions, and, when applied to the structure and phenomenology of the myosin II motor (chemo-mechanical transduction), resulted in a half-dozen realized expectations. These findings do much to substantiate the relevance of the hydrophobic and elastic consilient mechanisms to the protein-based machines of biology. 

The above three discussed protein-based machines—Complex III of the electron transport chain, ATP synthase/Fj-ATPase, and the myosin II motor of muscle contraction—represent the three major classes of energy conversion that sustain Life. Therefore, the facility with which the consilient mechanisms explain their function indeed support the thesis that biology s vital force arises from the coupled hydrophobic and elastic consilient mechanisms. 

---