ATP Synthase- All Experiments Point to Design

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As I posted earlier:

The ATP Synthase is a system that consists of two subsystems-> one for the flow of protons down an electrochemical gradient from the exterior to the interior and the other (a rotary engine) that generates ATP from ADP using the energy liberated by proton flow. These two processes are totally unrelated from a purely physiochemical perspective*- meaning there isn't any general principle of physics nor chemistry by which these two processes have anything to do with each other. Yet here they are.

How is this evidence for Intelligent Design? Cause and effect relationships as in designers often take two totally unrelated systems and intergrate them into one. The ordering of separate subsystems to produce a specific effect that neither can do alone. And those subsystems are composed of the ordering of separate components to achieve a specified function.

ATP synthase is not reducible to chance and necessity and also meets the criteria of design.

* Emergent collective properties, networks, and information in biology, page 23:

In the same vein, ATP synthesis in mitochondria can be conceived of and explained only because there is a coupling between ATP-synthase, the enzyme responsible for ATP synthesis, and the electrochemical potential. Hence ATP synthesis emerges out of this coupling. The activity of ATP-synthase alone could have in no way explained ATP synthesis. It is the merit of Mitchell, to have shown that it is precisely the interaction between two different physico-chemical events that generates this novel remarkable property. (italics in original)

Next we take a look inside ATP synthase-

“Thermodynamic efficiency and mechanochemical coupling of F1-ATPase”:

Abstract:

F1-ATPase is a nanosized biological energy transducer working as part of FoF1-ATP synthase. Its rotary machinery transduces energy between chemical free energy and mechanical work and plays a central role in the cellular energy transduction by synthesizing most ATP in virtually all organisms. However, information about its energetics is limited compared to that of the reaction scheme. Actually, fundamental questions such as how efficiently F1-ATPase transduces free energy remain unanswered. Here, we demonstrated reversible rotations of isolated F1-ATPase in discrete 120° steps by precisely controlling both the external torque and the chemical potential of ATP hydrolysis as a model system of FoF1-ATP synthase. We found that the maximum work performed by F1-ATPase per 120° step is nearly equal to the thermodynamical maximum work that can be extracted from a single ATP hydrolysis under a broad range of conditions. Our results suggested a 100% free-energy transduction efficiency and a tight mechanochemical coupling of F1-ATPase.

Highly effiecient, irreducibly complex, and no way- physiochemcially to get the two subunits to come together-> there's no attraction and no coupling.


See also:

Davies et al., “Macromolecular organization of ATP synthase and complex I in whole mitochondria,” Proceedings of the National Academy of Sciences

Tamás Beke-Somfai, Per Lincoln, and Bengt Nordén, “Double-lock ratchet mechanism revealing the role of [alpha]SER-344 in F0F1 ATP synthase,” Proceedings of the National Academy of Sciences