Complex V, also known as ATP synthase, is the final crucial component of the electron transport chain (ETC) in oxidative phosphorylation. It plays the central role in the synthesis of ATP, utilizing the energy stored by the proton motive force generated during electron transport in the ETC. The proton motive force consists of both a proton concentration gradient and an electric potential across the inner mitochondrial membrane. ATP synthase is an unusual enzyme that acts as both a proton pump and as a rotary molecular motor and consists of two main components: F0 and F1. The F0 component of complex V is embedded in the inner mitochondrial membrane and functions as a proton channel. It allows protons to flow back into the mitochondrial matrix from the intermembrane space, driven by the proton motive force. The flow of protons through F0 powers the rotation of the F1 component, which is critical for ATP synthesis. The F1 component is located within the mitochondrial matrix and houses the catalytic sites for ATP synthesis. It consists of five subunits, arranged in a hexameric ring structure. As protons flow through F0, it causes the rotation of the F1 component, leading to conformational changes that then promote the binding of ADP and Pi and the release of synthesized ATP. The mechanism of ATP synthesis by ATP synthase is often referred to as the "binding change" mechanism. As protons flow through F0, they cause rotation of the central stalk in F1. This rotation induces conformational changes in the three catalytic subunits of F1 (α, β, and γ subunits), allowing them to alternate between three different states: loose, tight, and open. In the loose state, ADP and Pi can bind to the catalytic sites. In the tight state, the bound ADP and Pi are brought closer together, facilitating the synthesis of ATP. Finally, in the open state, ATP is released from the catalytic sites. The rotation of the central stalk is driven by the flow of protons, and each full rotation of the stalk results in the synthesis of three molecules of ATP. Complex V plays a crucial role in energy coupling and metabolism, connecting the electron transport chain's energy release with ATP synthesis. The flow of electrons through the ETC generates a proton motive force by pumping protons from the mitochondrial matrix to the intermembrane space. This proton motive force, consisting of both a proton gradient and a membrane potential, provides the necessary chemical energy for ATP synthesis by ATP synthase. ATP synthase is itself regulated to match ATP synthesis with the cellular energy demands. One of the main regulatory mechanisms involves the availability of ADP and Pi. When the cell's ATP levels are low and ADP and Pi levels are high, ATP synthase is activated, promoting ATP synthesis to meet energy needs. Additionally, ATP synthase can be inhibited by high levels of ATP. When ATP levels are sufficient, ATP synthase slows down or stops ATP synthesis, preventing an unnecessary build-up of ATP. We provide a wide product range of research tools for investigating Complex V, including ATP5A antibodies, and ATP5H antibodies. Explore our full Complex V product range below and discover more, for less.