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Mitochondrial F1-ATPase is the catalytic core of the mitochondrial ATP synthase complex, responsible for synthesizing ATP using energy derived from a proton gradient across the inner mitochondrial membrane. It is a large, water-soluble protein complex composed of five different subunits: α, β, γ, δ, and ε, arranged in a α3β3γδε stoichiometry. The F1 portion protrudes into the mitochondrial matrix and contains all catalytic sites for ATP synthesis. It can also hydrolyze ATP under certain conditions.
Oligomycin binds to the Fo subunit, inhibiting proton flow. Bz-423 targets OSCP within FoF1, leading to superoxide generation and apoptosis. IF1 inhibits F1 ATPase hydrolytic activity.
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