Bacteriorhodopsin: mutating a biomaterial into an optoelectronic material

Abstract Bacteriorhodopsin (BR) is the key protein for the halobacterial photosynthetic capabilities and is one of the very rare molecules which occur in crystalline form in nature. Since its discovery, which was reported in 1971, many efforts have been made to exploit the obvious technical potential of this molecule. Successful application of gene technology methods for the modification of the physical function of a biomolecule was first demonstrated with BR. This approach points the way to a new class of materials derived from evolutionary optimized biomaterials by genetic re-engineering. Mutated BRs proved to have significant advantages over the wild type in optical applications. The current status of potential technical applications of BR is reviewed. BR is employed as a photoelectric, photochromic or energy-converting element. First systems now exist which demonstrate the successful integration of this new material into existing technologies. Analyzing the patents filed, which claim the processing or application of BR, gives an indication to areas where further technical uses are to be expected in the near future.

[1]  D. Oesterhelt,et al.  Rhodopsin-like protein from the purple membrane of Halobacterium halobium. , 1971, Nature: New biology.

[2]  D. Oesterhelt,et al.  Bacteriorhodopsin as a light‐drive ion exchanger? , 1976 .

[3]  Bacteriorhodopsin as a light-driven ion exchanger? , 1976, FEBS letters.

[4]  M. Montal,et al.  Electrical demonstration of rapid light-induced conformational changes in bacteriorhodopsin , 1977, Nature.

[5]  S. Caplan,et al.  Bacteriorhodopsin‐loaded charged synthetic membranes utilization of light energy to generate electrical current , 1977, FEBS letters.

[6]  J. Lanyi.  Halorhodopsin — a second retinal pigment in Halobacterium halobium , 1981 .

[7]  J. Spudich,et al.  Mechanism of colour discrimination by a bacterial sensory rhodopsin , 1984, Nature.

[8]  M. C. Nuss,et al.  Femtosecond spectroscopy of the first events of the photochemical cycle in bacteriorhodopsin , 1985 .

[9]  C. H. Brito Cruz,et al.  Direct observation of the femtosecond excited-state cis-trans isomerization in bacteriorhodopsin. , 1988, Science.

[10]  R. Henderson,et al.  Images of purple membrane at 2.8 A resolution obtained by cryo-electron microscopy. , 1988, Journal of molecular biology.

[11]  Richard Henderson,et al.  A model for the structure of bacteriorhodopsin based on high resolution electron cryomicroscopy , 1990 .

[12]  J. Lanyi,et al.  An efficient system for the synthesis of bacteriorhodopsin in Halobacterium halobium. , 1990, Gene.

[13]  R. Henderson,et al.  Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. , 1990, Journal of molecular biology.

[14]  R. Birge.  Photophysics and molecular electronic applications of the rhodopsins. , 1990, Annual review of physical chemistry.

[15]  R. Birge,et al.  Nature of the primary photochemical events in rhodopsin and bacteriorhodopsin. , 1990, Biochimica et biophysica acta.

[16]  R Henderson,et al.  The structure of bacteriorhodopsin and its relevance to the visual opsins and other seven-helix G-protein coupled receptors. , 1990, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.

[17]  N. Hampp,et al.  Bacteriorhodopsin: a biological material for information processing , 1991, Quarterly Reviews of Biophysics.

[18]  E. Bamberg,et al.  A unifying concept for ion translocation by retinal proteins , 1992, Journal of bioenergetics and biomembranes.

[19]  T. Miyasaka,et al.  Quantum Conversion and Image Detection by a Bacteriorhodopsin-Based Artificial Photoreceptor , 1992, Science.

[20]  V. Skulachev.  Interrelations of bioenergetic and sensory functions of the retinal proteins , 1993, Quarterly Reviews of Biophysics.

[21]  T. Miyasaka,et al.  Antibody-Mediated Bacteriorhodopsin Orientation for Molecular Device Architectures , 1994, Science.

[22]  T V Dyukova,et al.  Retinal-protein complexes as optoelectronic components. , 1994, Trends in biotechnology.

[23]  R Henderson,et al.  Three-dimensional structure of halorhodopsin at 7 A resolution. , 1995, Journal of molecular biology.

[24]  Felix T. Hong,et al.  Molecular sensors based on the photoelectric effect of bacteriorhodopsin: Origin of differential responsivity , 1997 .

[25]  J. Lanyi,et al.  Mechanism of Ion Transport across Membranes , 1997, The Journal of Biological Chemistry.

[26]  D. Oesterhelt,et al.  The structure and mechanism of the family of retinal proteins from halophilic archaea. , 1998, Current opinion in structural biology.

[27]  D. Oesterhelt,et al.  Closing in on bacteriorhodopsin: progress in understanding the molecule. , 1999, Annual review of biophysics and biomolecular structure.