Photorefractive Protein bacteriorhodopsin, BR , as a material forholographic data-recording
y María Gomariz
Grupo de Biomateriales. División de Óptica. Departamento de Ciencia deMateriales, Óptica y Tecnología Eectrónica, Universidad Miguel Hernández. C/ Avda. Universidad, s/n. Edif. Torrevaillo 03202-Elche, España.
División deMicrobiología, Departamento de Producción Vegetal y Microbiología, UniversidadMiguel Hernández. C/ Avda. Universidad, s/n. Edif. Torregaitán, 03202-Elche,España.
The search of materials of biological originwith specific estates of potential technologicapplications whose structure and functionscome out from a process of adaptiveevolution experienced by the organisms inextreme environments, is one of the mostactive fields in the modern biophysics.In short, the protein bacteriorhodopsin, actslike a protonic bomb whose photocycle hasdemonstrated interesting implications in thetechnologies of optic storage of informationby means of holographic methods.In the present work some results of theinvestigation undertaken by our group areexposed, consistent mainly in the study of the influence that working conditions (pH,state of aggregation of the environment,intensity and time of illumination, etc.) haveover photophysical and photochemical statesof bacteriorhodopsin as well as in thetracking of the possible presence of bacteriorhodopsin proteins andxantorhodopsin, in the salines of Santa Pola(Alicante, Spain).1.
For the bioengineering of the XXI century,learning from the benefits demonstrated bythe adaptive structures generated by naturalselection, and using proteins as functionalunits incorporating them in the moderntechnological devices, are two of the mostimportant challenges.In this sense, molecules as photoactiveproteins are able to transform the lightdirectly into an electric signal . Thisprocess implies the formation of an electricdipole and occur by changing proteinspectrum.Chlorophyll (in vegetables and bacteria) andrhodopsin (in animals and bacteria) are themost extended photosensitive biomoleculesin our planet whose role as converters of solar energy make them very well-known.The basic structure of the rhodopsin consistsof retinal molecules connected to proteins(opsins) with a specific structure by meansof a Schiff base. In almost all the naturalrhodopsins, the cromophore is the portion of retinal in the complex retinal-protein due toits high molar extinction coefficient, itsexcellent quantum yield and its shortisomerization time. The proteins and retinalthat separately absorb in the UV range whencombining, shift their spectrum of absorption to the visible region. It isnecessary to highlight that the proteincomplexes of the retinal transport ionsthrough the membranes, while chlorophyllproduces separations of electric charges.1