proton-transporting ATPase activity, rotational mechanism

Definition

Target type: molecularfunction

Enables the transfer of protons from one side of a membrane to the other according to the reaction: ATP + H2O + H+(in) -> ADP + phosphate + H+(out), by a rotational mechanism. [RHEA:57721]

Proton-transporting ATPase activity, rotational mechanism, involves the coordinated movement of multiple protein subunits to generate ATP from ADP and inorganic phosphate. This process is driven by the transmembrane movement of protons, which are pumped across a membrane by the enzyme. The enzyme consists of two main components: a membrane-bound F0 subunit and a peripheral F1 subunit. The F0 subunit forms a channel through the membrane, allowing protons to flow through it. This proton flow is coupled to the rotation of a central stalk within the F0 subunit. The central stalk is connected to the F1 subunit, which contains the catalytic sites for ATP synthesis. As the central stalk rotates, it interacts with the catalytic sites, causing them to change conformation and synthesize ATP. This mechanism can be described in three steps:

1. Proton Binding and Rotation: Protons bind to the F0 subunit, causing a conformational change that rotates the central stalk.

2. Stator-Rotor Interaction: The rotating central stalk interacts with the stationary F1 subunit, causing a conformational change in the catalytic sites.

3. ATP Synthesis: The conformational change in the catalytic sites promotes the formation of ATP from ADP and inorganic phosphate.

This rotational mechanism is highly efficient and is responsible for generating the majority of ATP in most living organisms.'
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Proteins (2)

Compounds (6)