ATP synthase (F₁F₀-ATP synthase) (ATP synthase)

ATP synthase (F₁F₀-ATP synthase) is the core enzyme responsible for ATP production in mycobacteria by utilizing the proton motive force (PMF) generated through the electron transport chain (ETC) during oxidative phosphorylation[1][3][8]. Key ETC components include NADH dehydrogenases (NDH-1, NDH-2), succinate dehydrogenase (SDH), menaquinone, cytochrome complexes, and fumarate reductase, supporting aerobic and anaerobic energy metabolism[1][3][7]. Mycobacteria are remarkable for their metabolic flexibility, especially adaptation to hypoxia and nutrient shifts, mediated via complex regulatory networks and metabolic remodeling[2][7]. Drugs such as bedaquiline and Q203 selectively inhibit mycobacterial energy metabolism, making ATP synthase and ETC enzymes prime targets for tuberculosis therapy[1][8]. In summary, "Mycobacterial energy production" should be mapped to specific molecular targets (primarily ATP synthase and select electron transport chain enzymes) for therapeutic and scientific purposes[1][8][3].

Other names

F₁F₀ ATP synthaseFF-ATP synthaseMycobacterial electron transport chainMycobacterial ETC

Inhibition of ATP synthase (inhibiting conversion of PMF to ATP by bedaquiline) Disruption of electron transport chain (Q203 inhibition of cytochrome bc₁, thioridazine, phenothiazines block NDH-2, SDH) Dissipation of proton motive force (by ionophores, some antibiotics) Depletion of ATP pool