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1 wrz 2001 · Key Points. ATP synthase is a ubiquitous, highly conserved enzyme that catalyses the formation of ATP from ADP and P i using a unique rotary motor mechanism. The enzyme is located in the...
26 lis 1999 · Adenosine triphosphate (ATP) synthase contains a rotary motor involved in biological energy conversion. Its membrane-embedded F 0 sector has a rotation generator fueled by the proton-motive force, which provides the energy required for the synthesis of ATP by the F 1 domain.
The ATP synthase, also called Complex V, has two major subunits designated F 0 and F 1. The F 0 part, bound to inner mitochondrial membrane is involved in proton translocation, whereas the F 1 part found in the mitochondrial matrix is the water soluble catalytic domain.
ATP synthase is composed of the F 1 and F 0 motor sharing a common rotary shaft (gray). A stator stalk connects two motors ( red ) that do not slip. The F 0 motor generates a rotary torque powered by the proton flow-enforcing F 1 motor to synthesize ATP.
3 sie 2021 · Nature Communications - F1Fo ATP synthase works using a rotary catalysis mechanism. Here, the authors report cryo-EM structures of Bacillus PS3 F1-ATPase encompassing the complete set of six...
1 sty 2003 · Most cellular ATP is synthesized from adenosine disphosphate (ADP) and P i by a ubiquitous coupling enzyme, the H + - transporting ATP synthase, in the terminal step of oxidative- and photo-phosphorylation. The ATP synthase is found embedded in the inner membrane of mitochondria, the thylakoid membrane of chloroplasts, and the plasma membrane ...
Three protein motors have been unambiguously identified as rotary engines: the bacterial flagellar motor and the two motors that constitute ATP synthase (F0F1 ATPase). Of these, the bacterial flagellar motor and F0 motors derive their energy from a transmembrane ion-motive force, whereas the F1 motor is driven by ATP hydrolysis.
