ATP synthase subunit beta, mitochondrial (ATP5F1B)

ATP synthase subunit beta is the primary catalytic component of the F1 domain within the ATP synthase complex (Complex V), located in the inner mitochondrial membrane [1, 7]. It orchestrates the synthesis of ATP from ADP and inorganic phosphate by utilizing the energy of a proton gradient through a unique rotational binding-change mechanism involving open, loose, and tight conformational states [17]. Beyond its fundamental role in mitochondrial bioenergetics, this subunit can translocate to the cell surface in certain conditions like cancer or hypoxia, where it serves as an ectopic receptor for ligands such as angiostatin to regulate angiogenesis [4, 13, 15]. Dysregulation or oxidative damage to the beta subunit is significantly linked to neurodegenerative disorders such as Alzheimer’s and Parkinson’s, as well as various metabolic and mitochondrial diseases [10, 12]. Because of its central role in cellular energy production, it is a significant target for diverse inhibitors, including polyphenols like resveratrol and antibiotics like aurovertin, though therapeutic application is often limited by the risk of systemic mitochondrial toxicity [1, 16].

Other names

ATP synthase F1 subunit betaATP5BBeta-chain adenosine triphosphate synthaseMitochondrial ATP synthase subunit betaATPSBATP synthase, H+ transporting, mitochondrial F1 complex, beta polypeptide

Inhibition of the catalytic F1 domain by binding to the beta subunit, which prevents the conformational transitions (open, loose, and tight states) and rotational movement of the gamma subunit required for ATP synthesis or hydrolysis [13, 17].