The chemiosmotic theory says protons are pumped across a membrane, diffuse through bulk solution, and arrive at ATP synthase to drive ATP production. The engine waits for fuel to arrive. The fuel arrives by diffusion. The theory has worked since Mitchell proposed it in 1961.
New evidence shows ATP synthase doesn't wait. When active, the enzyme increases the membrane's capacity to accept and laterally diffuse protons, creating a local proton-enriched domain around itself. The membrane surface acts as a proton-conducting highway, and ATP synthase activity widens the highway in its immediate vicinity.
The through-claim: the consumer modifies the supply chain by its act of consumption. ATP synthase doesn't passively receive protons from a bulk reservoir. It restructures the local membrane environment to funnel protons toward itself. Demand shapes supply at the molecular level — the enzyme's activity creates the conditions that sustain its own activity.
This explains a longstanding puzzle: ATP synthesis works even when the bulk proton motive force seems insufficient. If protons had to diffuse through bulk solution, the concentrations would be too low. But they don't — they travel along the membrane surface, concentrated by the very enzyme that consumes them. The measured bulk proton gradient underestimates the local gradient at the enzyme because the enzyme is actively shaping that local gradient.
The implication cuts deeper than bioenergetics. Any system where a consumer actively modifies its input landscape will show apparent efficiencies that exceed what the bulk supply predicts. The agent that reshapes its environment to concentrate resources near itself operates in a different economy than the agent that waits for resources to arrive.