ATP synthase function

A Membrane-Located ATP Synthase Functions as a Rotary Motor to Form ATP... 

The housing of the Fi-motor contains the heart of the ATP synthase function (when the y-rotor is driven clockwise by the Fo-motor) or ATPase... 

With this model, the energy-requiring step is not the formation of ATP but the conformational change that allows release of tightly bound ATP. The role of the a-subunits may be to maintain the functional conformation of the P-subunits. Another subtmit is sometimes associated with F this may regulate ATP synthase... 

F-ATPases (including the H+- or Na+-translocating subfamilies F-type, V-type and A-type ATPase) are found in eukaryotic mitochondria and chloroplasts, in bacteria and in Archaea. As multi-subunit complexes with three to 13 dissimilar subunits, they are embedded in the membrane and involved in primary energy conversion. Although extensively studied at the molecular level, the F-ATPases will not be discussed here in detail, since their main function is not the uptake of nutrients but the synthesis of ATP ( ATP synthase ) [127-130]. For example, synthesis of ATP is mediated by bacterial F-type ATPases when protons flow through the complex down the proton electrochemical gradient. Operating in the opposite direction, the ATPases pump 3 4 H+ and/or 3Na+ out of the cell per ATP hydrolysed. 

Deckers-Hebestreit, G. and Altendorf, K. (1996). The FoFi-type ATP synthases of bacteria structure and function of the F0 complex, Ann. Rev. Microbiol., 50, 791-824. 

Substances that functionally separate oxidation and phosphorylation from one another are referred to as uncouplers. They break down the proton gradient by allowing ions to pass from the intermembrane space back into the mitochondrial matrix without the involvement of ATP synthase. Uncoupling effects are produced by mechanical damage... 

Rotational catalysis by ATP synthase, BINDING CHANGE MECHANISM ROTATIONAL CORRELATION TIME CORRELATION FUNCTION ROTATIONAL DIFFUSION FLUORESCENCE... 

The synthesis of ATP is catalyzed by the enzyme ATP synthase (or FiFq-ATP synthase) the Fj portion of this enzyme was first isolated by Racker and coworkers in 1960 [4]. ATP synthase is present in abundance in the membranes of animal mitochondria, plant chloroplasts, bacteria and other organisms. ATP synthesized by our ATP synthase is transported out of mitochondria and used for the function of muscle, brain, nerve, liver and other tissues, for active transport, and for synthesizing myriad compounds needed by the cell. Since the pool of adenosine phosphates in the body is limited, the use of ATP must be continually compensated by its synthesis, and an active person synthesizes his own body weight of ATP every day. The synthesis of ATP is the most prevalent chemical reaction in the body [5]. This is indeed a very important reaction. How exactly does it occur ... 

The molecular basis of site-site cooperativity in ATP synthase still remains unelucidated [46], and the absence of any direct evidence for cooperativity (despite almost three decades of effort) is explained, within the framework of the torsional mechanism, by the fact that site-site cooperativity does not exist in the physiological, steady state mode of functioning. Since, according to the torsional mechanism, no rotation takes place in uni-site or bi-site catalysis... 

In chemical terms the photoinduced electron transfer results in transfer of an electron across the photosynthetic membrane in a complex sequence that involves several donor-acceptor molecules. Finally, a quinone acceptor is reduced to a semiquinone and subsequently to a hydroquinone. This process is accompanied by the uptake of two protons from the cytoplasma. The hydroquinone then migrates to a cytochrome be complex, a proton pump, where the hydroquinone is reoxidized and a proton gradient is established via transmembrane proton translocation. Finally, an ATP synthase utilizes the proton gradient to generate chemical energy. Due to the function of tetrapyrrole-based pigments as electron donors and quinones as electron acceptors, most biomimetic systems utilize some... 

S ATP -I- 1 D-myo-inositol hexakisphosphate <1> (<1>, enzyme is responsible for the biosynthesis of diphospho-myo-inositol pentakisphosphate. The enzyme also has a ATP synthase activity, implying that 5-diphos-pho-1 D-myo-inositol pentakisphosphate functions as high-energy phosphate donor [1]) (Reversibility r <1> [1]) [1]... 

Ca2+ cycling into and out of the mitochondria leads to NAD depletion and a fall in ATP. The entry of Ca2+ into the mitochondria dissipates the potential difference across the mitochondrial membranes and so inhibits the function of ATP synthase, which relies on the charge difference across the membrane (Fig. 6.13 and 7.60). Export of Ca2+ from the mitochondrial matrix may occur and be stimulated by some chemicals. However, this will lead to repeated cycling, which damages the membrane and further compromises ATP synthesis. The export of Ca2+ also uses up ATP as a result of the Ca2+ ATPases involved. Hence ATP levels fall. 

The reaction catalyzed by F-type ATPases is reversible, so a proton gradient can supply the energy to drive the reverse reaction, ATP synthesis (Fig. 11-40). When functioning in this direction, the F-type ATPases are more appropriately named ATP synthases. ATP synthases are central to ATP production in mitochondria during oxidative phosphorylation and in chloroplasts during photophosphorylation, as well as in eubacteria and archaebacteria. The proton gradient needed to drive ATP synthesis is produced by other types of proton pumps powered by substrate oxidation or sunlight. As noted above, we return to a detailed description of these processes in Chapter 19. 

FIGURE 19-1 Biochemical anatomy of a mitochondrion. The convolutions (cristae) of the inner membrane provide a very large surface area. The inner membrane of a single liver mitochondrion may have more than 10,000 sets of electron-transfer systems (respiratory chains) and ATP synthase molecules, distributed over the membrane surface. Heart mitochondria, which have more profuse cristae and thus a much larger area of inner membrane, contain more than three times as many sets of electron-transfer systems as liver mitochondria. The mitochondrial pool of coenzymes and intermediates is functionally separate from the cytosolic pool. The mitochondria of invertebrates, plants, and microbial eukaryotes are similar to those shown here, but with much variation in size, shape, and degree of convolution of the inner membrane. 

For the continued synthesis of ATP, the enzyme must cycle between a form that binds ATP very tightly and a form that releases ATP. Chemical and crystallographic studies of the ATP synthase have revealed the structural basis for this alternation in function. 

What is the mechanism by which ATPase transporters function We still do not know.550 The pumping cycles for the Na+,K+- ATPase and the Ca2+- ATPase are similar although different in details. The ATPases are reversible and with suitable ionic gradients will work as ATP synthases.551 A strictly hypothetical model for the Na+,... 

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