Abstract
Proteins and lipids are the building blocks of biological membranes. In the past and at present, only the lipids in the form of bilayers, vesicles, and thin films found/find applications in technology. However, the membrane proteins are responsible for most of the vital processes accomplished by membranes. These proteins, which are in part or completely embedded in the lipid matrix mainly via helical amino acid regions, act as pores (channels), pumps, and transport systems for ions and nutriments. Furthermore, they are very selective receptors for hormones, neurotransmitter, drugs, medicine, and they mediate specific cell-cell recognition. Biological membranes can be regarded as the largest and most active organ in a living organism. They are the site of many vital processes for life. Photosynthesis and oxidative phosphorylation, the two most important energy conversion processes in biological systems as well as sensory transduction are carried out by membranes, i.e., by the proteins residing in the membrane. Therefore, it can be expected that in the near future membrane proteins will gain great importance in biotechnology. In the following, the putative capacity of membrane proteins to serve as biosensor, biochip, and bioconverter of energy will be discussed by referring to the light-driven proton pump bacteriorhodopsin.
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References
D. Oesterhelt and W. Stoeckenius, Functions of a new photoreceptor membrane, Proc. Nat, Acad. Sci. USA 70:2853–2857 (1973).
N. Dencher and M. Wilms, Flash photometric experiments on the photo-chemical cycle of bacteriorhodopsin, Biophys. Struct. Mechanism 1:259–271 (1975).
S. Grzesiek and N. A. Dencher, Time-course and stoichiometry of H+-release and uptake during the photochemical cycle of bacteriorhodopsin, FEBS Lett. 208:337–342 (1986).
A. Matsuno-Yagi and Y. Mukohata, Two possible roles of bacteriorhodop-sin; a comparative study of strains of Halobacterium halobium differing in pigmentation, Biochem. Biohys. Res. Commun. 78:237–243 (1977).
B. Schobert and J. K. Lanyi, Halorhodopsin is a light-driven chloride pump, J. Biol. Chem. 257:10306–10313 (1982).
A. Blanck and D. Oesterhelt, The halo-opsin gene. II. Sequence, primary structure of halorhodopsin and comparison with bacteriorhodopsin, EMBO J. 6: 265–273 (1987).
N. A. Dencher, The five retinal-protein pigments of halobacteria: Bacteriorhodopsin, Halorhodopsin, P 565, P 370, and slow-cycling rhodopsin, Photochem. Photobiol. 38:753–767 (1983).
J. Briggs, Biosensors emerge from the laboratory, Nature 329:565–566 (1987).
N. A. Dencher, P. A. Burghaus, and S. Grzesiek, Determination of the net proton-hydroxide ion permeability across vesicular lipid bilayers and membrane proteins by optical probes, Methods Enzymol. 127:746–760 (1986).
F. T. Hong and M. Conrad, The bacteriorhodopsin as a prototype molecu-lar electronic device, in: “Proceedings of the 3rd International Symposium on Molecular Electronic Devices”, F. L. Carter and H. Wohltjen, ed., North-Holland, Amsterdam (1987).
F. T. Hong, The bacteriorhodopsin model membrane system as a prototype molecular computing element, BioSystems 19:223–236 (1986).
H. Schindler, Formation of planar bilayers from artificial or native membrane vesicles, FEBS Lett. 122:77–79 (1980).
E. Bamberg, N. A. Dencher, A. Fahr, and M. P. Heyn, Transmembraneous incorporation of photoelectrically active bacteriorhodopsin in planar lipid bilayers, Proc. Natl. Acad. Sci. USA 78:7502–7506 (1981).
D. Braun, N. A. Dencher, A. Fahr, M. Lindau, and M. P. Heyn, Nonlinear voltage dependence of the light-driven proton pump current of bacteriorhodopsin, Biophys. J. 53 (1988).
S.-B. Hwang and W. Stoeckenius, Purple membrane vesicles: Morphology and proton translocation, J. Membrane Biol. 33:325–350 (1977).
E. Racker, Reconstitution of membrane processes, Methods Enzymol. 55:699–711 (1979).
P. W. M. van Dijck and K. van Dam, Bacteriorhodopsin in phospholipid vesicles, Methods Enzymol 88:17–25 (1982).
N. A. Dencher, Spontaneous transmembrane insertion of membrane proteins into lipid vesicles facilitated by short-chain lecithins, Biochemistry 25:1195–1200 (1986).
R. Casadio and W. Stoeckenius, Effect of protein-protein interaction on light adaptation of bacteriorhodopsin, Biochemistry 19:3374–3381 (1980).
N. A. Dencher and A. Wach, unpublished work.
J. L. Rigaud, A. Bluzat, and S. Bushlen, Incorporation of bacteriorho-dopsin into large unilamellar liposomes by reverse phase evaporation, Biochem. Biophys. Res. Commun. 111:373–382 (1983).
E. Racker, B. Violand, S. O’Neal, M. Alfonzo, and J. Telford, Reconsti-tution, a way of biochemical research; some new approaches to membrane-bound enzymes, Arch. Biochem. Biophys. 198:470–477 (1979).
M. P. Heyn and N. A. Dencher, Reconstitution of monomeric bacteriorho-dopsin into phospholipid vesicles, Methods Enzymol. 88:31–35 (1982).
N. A. Dencher and M. P. Heyn, Preparation and properties of monomeric bacteriorhodopsin, Methods Enzymol. 88:5–10 (1982).
J. Krupinski and G.G. Hammes, Steady-state ATP synthesis by bacterio-rhodopsin and chloroplast coupling factor co-reconstituted into asolectin vesicles, Proc. Natl. Acad. Sci. USA 83:4233–4237 (1986).
N. A. Dencher, The light-energized H+-pump bacteriorhodopsin: A model system for functional transmembrane reconstitution of ion channels, receptors, and pumps, in: “Receptors and Ion Channels”, Y. A. Ovchinnikov and F. Hucho, ed., Walter de Gruyter, Berlin/New York, pp. 265–273 (1987).
N. A. Dencher, Gentle and fast transmembrane reconstitution of membrane proteins, Methods Enzymol., in press (1988).
A. W. Scotto and D. Zakim, Reconstitution of membrane proteins: cata-lysis by cholesterol of insertion of integral membrane proteins into preformed lipid bilayers, Biochemistry 25:1555–1561 (1986).
M. P. Heyn, P.-J. Bauer, and N. A. Dencher, A natural CD label to probe the structure of the purple membrane from Halobacterium halobium by means of exciton coupling effects, Biochem. Biophys. Res. Commun. 67:897–903 (1975).
R. J. Cherry, Rotational and lateral diffusion of membrane proteins, Biochim. Biophys. Acta 559:289–327 (1979).
M. P. Heyn, R. J. Cherry, and N. A. Dencher, Lipid-protein interactions in bacteriorhodopsin-dimyristoylphosphatidylcholine vesicles, Biochemistry 20:840–849 (1981).
N. A. Dencher and M. P. Heyn, Bacteriorhodopsin monomers pump protons, FEBS Lett. 108:307–310 (1979).
N. A. Dencher, K.-D. Kohl, and M. P. Heyn, Photochemical cycle and light-dark adaptation of monomeric and aggregated bacteriorhodopsin in various lipid environments, Biochemistry 22:1323–1334 (1983),
S. Grzesiek and N. A. Dencher, Monomeric and aggregated bacteriorhodop-sin: single-turnover transport efficiency and photochemistry, Proc. Natl. Acad. Sci. USA, submitted (1988).
M. Shinitzky and Y. Barenholz, Fluidity parameters of lipid regions determined by fluorescence polarization, Biochim. Biophys. Acta 515:367–394 (1978).
M. Rehorek, N. A. Dencher, and M. P. Heyn, Fluorescence energy transfer from diphenylhexatriene to bacteriorhodopsin in lipid vesicles, Biophys. J. 43:39–45 (1983).
M. Rehorek, N. A. Dencher, and M. P. Heyn, Long-range lipid-protein interactions. Evidence from time-resolved fluorescence depolarization and energy transfer experiments with bacteriorhodopsin-dimyristoylphosphatidylcholine vesicles, Biochemistry 24:5980–5988 (1985).
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Dencher, N.A. (1988). Biotechnological Application of Membrane Proteins Reconstituted Into Vesicular and Planar Lipid Bilayers. In: Gaber, B.P., Schnur, J.M., Chapman, D. (eds) Biotechnological Applications of Lipid Microstructures. Advances in Experimental Medicine and Biology, vol 238. Springer, New York, NY. https://doi.org/10.1007/978-1-4684-7908-9_21
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DOI: https://doi.org/10.1007/978-1-4684-7908-9_21
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