Do you have a cite to the literature from which you took your ATP claim?Ã‚Â Thanks
I will do a quick and dirty post. I will engage you more but I don't want rapid fire questions without feedback from you. video
ItÃ¢â‚¬â„¢s not just figurative speech to call ATP synthase a rotary motor. It actually generates torque (the subject of the paper in Nature sited below). The authors compared it to a Wankel engine Ã¢â‚¬â€œ the kind that powers a Mazda car, and used the word Ã¢â‚¬Å“motorÃ¢â‚¬Â 30 times in the paper. They said the first studies of this molecular machine revealed it Ã¢â‚¬Å“resembling a three-chambered molecular Wankel engine, therefore strongly suggested that rotation, rather than alternation, was natureÃ¢â‚¬â„¢s choice, and that the synthesis of ATP might be mechanically driven by rotation....Ã¢â‚¬Â Synthesis of ATP (thus the name) is its job. ATP (adenosine triphosphate) is the energy currency for all of life. The ATP molecule is a nucleotide with extra phosphate groups attached. It requires energy to attach the phosphate groups; energy is liberated when they are removed. Most molecular processes in the cell (and in all of life) use that liberated energy that comes from ATP. Plants use it for photosynthesis; animals use it for respiration. Quadrillions of these rotary engines in a human body manufacture ATP constantly, day and night, to keep those processes operational. If they suddenly stopped, you would be dead before you hit the floor.
ATP synthase has several parts; a rotor, a stator, and a camshaft. ItÃ¢â‚¬â„¢s actually two motors in one. The top half (called F1) is a three-chambered assembly factory that pushes the phosphates onto the nucleotide. Three pairs of lobes in this stepping motor turns loading ADP and phosphate, assembling them, and releasing ATP molecules. They are powered underneath by a waterwheel-like rotating motor that runs on proton motive force Taking advantage of the ever-present Brownian motion and electrostatic interactions, the protons turn the wheel. This simultaneously turns a coupled camshaft-like mechanism that protrudes into the top half, which transfers the torque to the ATP-assembling lobes. The engine can work in either direction, constructing ATP molecules or breaking them down, depending on the concentration gradient.
Scientists have been intrigued by the mismatch of gear ratios between the top and bottom halves of the engine. In some animals, for instance, there are 11 units in the rotating half, but 3 in the top half. This implies some transfer of elastic energy in the camshaft. Whatever is happening, it works: scientists say this machine approaches 100% efficiency. For a taste of the discussion from the paper for those who know physics, they are discussing the match between the energy needed for ATP hydrolysis and the mechanical work done by the motor. source
We know that getting 3 positive mutations is sequences in beyond what random mutation and natural selection can do base on empirical data (malaria). How many mutations would be required to make this- many. What is the evolutionary pathway required? It is well beyond what evolution can do.
This is fairly new finding. Look at the machinery required to make ATP. nature link
Scientist marvel at the design of the process.
ATP synthase (FOF1) is a molecular machine that combines the electrical, mechanical and chemical aspects of enzyme function.Ã‚Â These are neatly separated, readily attributed to its different subunits, and reasonably well understood thanks to a wealth of structural and kinetic data.Ã‚Â However, understanding the enzyme fully at a molecular level will require considerable efforts, both experimental and theoretical.Ã‚Â There are five outstanding issues.... Only when we have solved these problems will we come close to a full understanding of this remarkable piece of cellular machinery.
The match implies 100% efficiency for the conversion of the Gibbs free energy of ATP hydrolysis into mechanical work performed on the elastically strained filament.Ã‚Â This is not surprising given the approximate thermodynamic equilibrium of the enzyme (long)-filament construct.Ã‚Â It is more informative to say that there is no slip between ATP hydrolysis in F1 and rotation in FO under the given conditions.2Ã‚Â Rotary slip in FOF1 in chloroplasts and bacteria has been detected, but only under single-site occupancy, that is, at nucleotide concentrations significantly below 100 nM.Ã‚Â The momentary torque can be larger (for example, during a particular power stroke) or smaller (during a kinetic dwell) than its equilibrium average.Ã‚Â This may account for the still puzzling independence of the torque from the ATP concentration in the nanomolar to millimolar range (see ref. 2 for a review).Ã‚Â It is worth mentioning that the other technique for determining the torque from the rate of rotation underestimates its magnitude because it neglects viscous flow coupling between the filament and the enzyme-supporting surface.