Proton pore

Thermogenin (uncoupler protein), a proton pore of 19-30, 23-22 mitochondrial inner membrane... 

Fig. 19-17), the electrochemi- 192°-1992 cal energy inherent in the difference in proton concentration and separation of charge across the inner mitochondrial membrane—the proton-motive force—drives the synthesis of ATP as protons flow passively back into the matrix through a proton pore associated with ATP synthase. To emphasize this crucial role of the proton-motive force, the equation for ATP synthesis is sometimes written... 

The enzyme responsible for ATP synthesis in chloroplasts is a large complex with two functional components, CF0 and CFi (C denoting its location in chloroplasts). CF0 is a transmembrane proton pore composed of several integral membrane proteins and is homologous to mitochondrial F0. CFi is a peripheral... 

Powell, B., Graham, L. A., and Stevens, T. H. (2000). Molecular characterization of the yeast vacuolar H+-ATPase proton pore./. Biol. Chem. 275, 23654—23660. 

The ATP synthase is composed of two components an integral membrane protein complex (CF0) that contains a proton pore and an extrinsic protein complex (CFO that synthesizes ATP. CF0 contains four different types of subunits I, II, III, and IV. The proton pore is composed of multiple copies of subunit II. Subunit IV (not shown) binds CF0 to CFj. CFj consists of five different subunits a, fi, y S, and e. 

As 2 electrons move from each water molecule to NADP1 (blue arrows), about two H+ are pumped from the stroma into the thylakoid lumen. Two additional H+ are generated within the lumen by the oxygen-evolving complex. The flow of protons through the proton pore in CF0 drives the synthesis of ATP in CF (MSP = manganese stabilizing protein ph = pheophytin Fd = ferredoxin FNR = ferredoxin-NADP oxidoreductase)... 

The Fo complex making up the proton pore is composed of three subunits, a, b, and c, in the proportion ab2Cio-i2- Subunit c is a small (M 8,000), very hydrophobic polypeptide, consisting almost entirely of two transmembrane helices, with a small loop extending from the matrix side of the membrane. The crystal structure of the yeast FqFi, solved in 1999, shows the arrangement of the c subunits. The yeast complex has ten c subunits, each with two transmembrane helices roughly perpendicular to the plane of the membrane and arranged in two concentric circles (Fig. 19-23d, e). The... 

The pumping of protons generates an electrochemical gradient (Ap) across the membrane composed of the membrane potential and the proton gradient. ATP synthase contains a proton pore through the inner mitochondrial membrane and a catalytic headpiece that protrudes into the matrix. As protons are driven... 

Marrink, S.J., Jahnig, F., Berendsen, H.J.C. Proton transport across transient single-file water pores in a lipid membrane studied by molecular dynamics simulations. Biophys. J. 71 (1996) 632-647. 

Strong acids are able to donate protons to a reactant and to take them back. Into this class fall the common acids, aluminum hahdes, and boron trifluoride. Also acid in nature are silica, alumina, alumi-nosihcates, metal sulfates and phosphates, and sulfonated ion exchange resins. They can transfer protons to hydrocarbons acting as weak bases. Zeolites are dehydrated aluminosilicates with small pores of narrow size distribution, to which is due their highly selective action since only molecules small enough to enter the pores can reacl . 

ATP synthase actually consists of two principal complexes. The spheres observed in electron micrographs make up the Fj unit, which catalyzes ATP synthesis. These Fj spheres are attached to an integral membrane protein aggregate called the Fq unit. Fj consists of five polypeptide chains named a, j3, y, 8, and e, with a subunit stoichiometry ajjSaySe (Table 21.3). Fq consists of three hydrophobic subunits denoted by a, b, and c, with an apparent stoichiometry of ajbgCg.ig- Fq forms the transmembrane pore or channel through which protons move to drive ATP synthesis. The a, j3, y, 8, and e subunits of Fj contain 510, 482, 272, 146, and 50 amino acids, respectively, with a total molecular mass... 

Figure 8. Three types of polarization of Mn02 (1) J]c (H+ solid), due to proton diffusion in solid (2) rja, due to the solution-solid interface (3) 7/t (ApH), due to a pH change of the electrolyte in the pores.

Ammonium salts of the zeolites differ from most of the compounds containing this cation discussed above, in that the anion is a stable network of A104 and Si04 tetrahedra with acid groups situated within the regular channels and pore structure. The removal of ammonia (and water) from such structures has been of interest owing to the catalytic activity of the decomposition product. It is believed [1006] that the first step in deammination is proton transfer (as in the decomposition of many other ammonium salts) from NH4 to the (Al, Si)04 network with —OH production. This reaction is 90% complete by 673 K [1007] and water is lost by condensation of the —OH groups (773—1173 K). The rate of ammonia evolution and the nature of the residual product depend to some extent on reactant disposition [1006,1008]. 

Because the pore dimensions in narrow pore zeolites such as ZSM-22 are of molecular order, hydrocarbon conversion on such zeolites is affected by the geometry of the pores and the hydrocarbons. Acid sites can be situated at different locations in the zeolite framework, each with their specific shape-selective effects. On ZSM-22 bridge, pore mouth and micropore acid sites occur (see Fig. 2). The shape-selective effects observed on ZSM-22 are mainly caused by conversion at the pore mouth sites. These effects are accounted for in the hydrocracking kinetics in the physisorption, protonation and transition state formation [12]. 

Alkene protonation at pore mouths can exclusively lead to secondary carbenium ions. In addition, the alkene standard protonation enthalpies increase with the number of carbon atoms inside the micropore because charge dispersive effects are supposed to be more effective on carbon atoms inside the micropores. 

Figure 2. Transition state complex in the ethanol + 2-pentanol 8, 2 reaction activated by the proton at the chaimel intersection of H21SM-5 [14]. The zeolite pore structure is represented as a wire-frame section of the intersecting channels produced by the MAPLE V software package. The zeolite proton that activates the 2-pentanol molecule is marked with. ...

Recent studies by Crompton et al. have shown that oxidant stress may open a Ca-sensitive, non-selective pore in the inner mitochondrial membrane that is blocked by cyclosporin A (Crompton, 1990 Crompton and Costi, 1990). This pore opening results in massive mitochondrial swelling, dissipation of the transmembrane proton gradient and disruption of mitochondrial energy production (Crompton et al., 1992). Since mitochondria may play a role as a slow, high-capacity cytosolic calcium buffer (Isenberg et al., 1993), disruption of mitochondrial function may also contribute to calcium overload and cell injury. 

Figure 2.9.3 shows typical maps [31] recorded with proton spin density diffusometry in a model object fabricated based on a computer generated percolation cluster (for descriptions of the so-called percolation theory see Refs. [6, 32, 33]).The pore space model is a two-dimensional site percolation cluster sites on a square lattice were occupied with a probability p (also called porosity ). Neighboring occupied sites are thought to be connected by a pore. With increasing p, clusters of neighboring occupied sites, that is pore networks, begin to form. At a critical probability pc, the so-called percolation threshold, an infinite cluster appears. On a finite system, the infinite cluster connects opposite sides of the lattice, so that transport across the pore network becomes possible. For two-dimensional site percolation clusters on a square lattice, pc was numerically found to be 0.592746 [6]. 

Fig. 2.9.3 Proton spin density diffusometry in a two-dimensional percolation model object [31]. The object was initially filled with heavy water and then brought into contact with an H2O gel reservoir, (a) Schematic drawing ofthe experimental set-up. The pore space is represented in white, (b) Maps ofthe proton spin density that were recorded after diffusion times t varying from 1.5 to 116 h. Projections of the...

Fig. 2.9.13 Qu asi two-dimensional random ofthe percolation model object, (bl) Simulated site percolation cluster with a nominal porosity map of the current density magnitude relative p = 0.65. The left-hand column refers to simu- to the maximum value, j/jmaK. (b2) Expedited data and the right-hand column shows mental current density map. (cl) Simulated NMR experiments in this sample-spanning map of the velocity magnitude relative to the cluster (6x6 cm2), (al) Computer model maximum value, v/vmax. (c2) Experimental (template) for the fabrication ofthe percolation velocity map. The potential and pressure object. (a2) Proton spin density map of an gradients are aligned along the y axis, electrolyte (water + salt) filling the pore space...

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