FoF1ATPsyntazy

FoF1-ATP synthase, also known as F1Fo-ATP synthase or ATP synthase, is a complex enzyme found in the inner mitochondrial membrane and bacterial plasma membrane. It plays a crucial role in cellular respiration and energy production. The enzyme is composed of two main parts: the F1 portion, which is embedded in the membrane, and the Fo portion, which protrudes into the intermembrane space. The F1 portion consists of five subunits: alpha, beta, gamma, delta, and epsilon. The Fo portion consists of three subunits: a, b, and c. The enzyme catalyzes the synthesis of adenosine triphosphate (ATP) from adenosine diphosphate (ADP) and inorganic phosphate (Pi) using the energy derived from the proton gradient across the membrane. The enzyme is inhibited by oligomycin, a macrolide antibiotic, and is activated by uncouplers, which dissipate the proton gradient. FoF1-ATP synthase is essential for the production of ATP, which is the primary energy currency of the cell.