Membranes proton pumping

Figure 5 The catalytic cycle and its linkage to proton translocation. States R through Or are equivalent to those in Figure 4. Large arrows denote translocation of one proton across the membrane (proton pumping). For details, see the text...

Pedersen BP, Buch-Pedersen MJ, Morth JP, Palmgren MG, Nissen P. Crystal structure of the plasma membrane proton pump. Nature 2007 450 1111-1114. 

Shi LC, Ahmed MAM, Zhang WR et al (2009) Three-dimensional solid-state NMR study of a seven-helical integral membrane proton pump-structural insights. J Mol Biol 386 1078-1093... 

L. Shi, M.A.M. Ahmed, W. Zhang, G. Whited, L.S. Brown, V. Ladizhansky, Three-dimensional solid-state NMR study of a seven-hehcal integral membrane proton pump—structural insights, J. Mol. Biol. 386 (2009) 1078—1093. 

C.L. Slayman, Charge-transport characteristics of a plasma membrane proton pump in Membranes and Transport, vol. 1 (Plenum Press, New York, 1982) pp. 485 90... 

In addition to binding to sialic acid residues of the carbohydrate side chains of cellular proteins that the virus exploits as receptors, hemagglutinin has a second function in the infection of host cells. Viruses, bound to the plasma membrane via their membrane receptors, are taken into the cells by endocytosis. Proton pumps in the membrane of endocytic vesicles that now contain the bound viruses cause an accumulation of protons and a consequent lowering of the pH inside the vesicles. The acidic pH (below pH 6) allows hemagglutinin to fulfill its second role, namely, to act as a membrane fusogen by inducing the fusion of the viral envelope membrane with the membrane of the endosome. This expels the viral RNA into the cytoplasm, where it can begin to replicate. 

ITowever, membrane proteins can also be distributed in nonrandom ways across the surface of a membrane. This can occur for several reasons. Some proteins must interact intimately with certain other proteins, forming multisubunit complexes that perform specific functions in the membrane. A few integral membrane proteins are known to self-associate in the membrane, forming large multimeric clusters. Bacteriorhodopsin, a light-driven proton pump protein, forms such clusters, known as purple patches, in the membranes of Halobacterium halobium (Eigure 9.9). The bacteriorhodopsin protein in these purple patches forms highly ordered, two-dimensional crystals. 

FIGURE 10.17 Proton pumps cluster on the ruffled border of osteoclast cells and function to pump protons into the space between the cell membrane and the bone surface. High proton concentration in this space dissolves the mineral matrix of the bone. 

When light-driven proton pumping across the thylakoid membrane occurs, a concomitant efflux of Mg ions from vesicles into the stroma is observed. This efflux of Mg somewhat counteracts the charge accumulation due to H ... 

C1C-6 is a late endosomal chloride transporter. Its disruption in mice led to lysosomal storage disease. C1C-7 is expressed in late endosomes and lysosomes. It needs Ostml as (3-subunit [3]. The disruption of either C1C-7 or Ostml in mice and man leads to severe osteopetrosis, retinal degeneration, and a severe lysosomal storage disease. ClC-7/Ostml is highly expressed in osteoclasts. In these cells, it is inserted together with the proton pump into the specialized plasma membrane ( ruffled border ) that faces the reabsorption lacuna. Osteoclasts are still present in C1C-7 knockout... 

The Langmuir-Blodged (LB) technique allows one to form a monolayer at the water surface and to transfer it to the surface of supports. Formation of the BR monolayer at the air/water interface, however, is not a trivial task, for it exists in the form of membrane fragments. These fragments are rather hydrophilic and can easily penetrate the subphase volume. In order to decrease the solubility, the subphase usually contains a concentrated salt solution. The efficiency of the film deposition by this approach (Sukhorukov et al. 1992) was already shown. Nevertheless, it does not allow one to orient the membrane fragments. Because the hydrophilic properties of the membrane sides are practically the same, fragments are randomly oriented in opposite ways at the air/water interface. Such a film cannot be useful for this work, because the proton pumping in the transferred film will be automatically compensated i.e., the net proton flux from one side of the film to the other side is balanced by a statistically equal flux in the opposite direction. 

FIG. 20 Schematic of device for light-addressable proton pumping. (1) BR containing membrane, (2,3) working sections, (4-6) electrodes, and (7) light source. 

Each of the respiratory chain complexes I, III, and IV (Figures 12-7 and 12-8) acts as a proton pump. The inner membrane is impermeable to ions in general but particularly to protons, which accumulate outside the membrane, creating an electrochemical potential difference across the membrane (A iH )-This consists of a chemical potential (difference in pH) and an electrical potential. 

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