Final answer:
The binding change mechanism of ATP production was proposed by Paul Boyer and involves conformational changes in the F1Fo ATP synthase enzyme to synthesize ATP, powered by a proton gradient as described by Peter Mitchell's chemiosmotic theory.
Step-by-step explanation:
The binding change mechanism of ATP production, which explains how ATP is generated in the F1Fo ATP synthase, was proposed by Paul Boyer. This mechanism operates through a process in which the enzyme undergoes conformational changes in three states: the loose-state, the tight-state, and the open-state. Each state allows the enzyme to interact differently with ADP and inorganic phosphate to facilitate the synthesis of ATP, which is a critical process for cellular energy.
The energy required for the ATP synthesis is provided by a proton gradient across the mitochondrial membrane, which was first described by Peter Mitchell in his chemiosmotic theory. The conformational changes in the F1Fo ATP synthase protein are driven by the flow of protons down this gradient, catalyzing the conversion of ADP and inorganic phosphate into ATP.