ATP synthasis

ATP synthasis est enzymum, quod ex ADP et phosphato inorganico (P_i) energiam cellulae vel quorundam bacteriorum conservantem ATP (adenosinum triphosphoricum) generat^[1] (synthesis ATP). Reactio chemica est:

ADP + P_i + H⁺_ext ⇌ ATP + H₂O + H⁺_int

Reactio simul est gradus terminalis spirationis internae, phosphorylationis oxydativae.

ATP synthasis ex compluribus partibus constituta est, et partes suae de compluribus genibus pendent. Complexus ATP synthasis intra membrana mitochondriali interna (vel bacterium) in ancoris stant.

Physiologia

ATP synthasis F₁F₀ est machinamentum motorium minimum. Rotationibus dextrorsum functio est ATP synthasis, at contrarie sinistrorsum agit ATPasis et antlia H⁺^[2].

Notae

↑ Okuno D., Iino R., Noji H. (Iun 2011). "Rotation and structure of FoF1-ATP synthase". Journal of biochemistry 149 (6): 655-64
↑ Mendoza-Hoffmann F., Zarco-Zavala M., et al. (Oct 2018). "Control of rotation of the F 1 F O-ATP synthase nanomotor by an inhibitory α-helix from unfolded ε or intrinsically disordered ζ and IF 1 proteins". Journal of bioenergetics and biomembranes 50 (5): 403-24

Plura legere si cupis

Paul D Boyer, "Catalytic site forms and controls in ATP synthase catalysis", Biochimica et Biophysica Acta (BBA) - Bioenergetics, 2000(1458): 252-262
Ian N Watt, Martin G Montgomery, Michael J Runswick, Andrew G W Leslie, John E Walker. "Bioenergetic cost of making an adenosine triphosphate molecule in animal mitochondria", Proc Natl Acad Sci U S A, 2010: 16823-16827

Nexus interni

[1] Okuno D., Iino R., Noji H. (Iun 2011). "Rotation and structure of FoF1-ATP synthase". Journal of biochemistry 149 (6): 655-64

[2] Mendoza-Hoffmann F., Zarco-Zavala M., et al. (Oct 2018). "Control of rotation of the F 1 F O-ATP synthase nanomotor by an inhibitory α-helix from unfolded ε or intrinsically disordered ζ and IF 1 proteins". Journal of bioenergetics and biomembranes 50 (5): 403-24

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