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Part of the book series: Biological and Medical Physics, Biomedical Engineering ((BIOMEDICAL))

Conversion of sunlight into energy or information and their storage on a chemical level is essential for life on earth. An important family of chromoproteins performing these tasks is that of retinal binding proteins. Prominent examples are rhodopsin (Rh) [1,2] as the visual pigment in vertebrate and invertebrate animals, the archaeal rhodopsins bacteriorhodopsin (BR) [3] as a light driven proton pump, halorhodopsin (HR) [4,5] as a light driven chloride pump, sensory rhodopsin I and II (SRI, SRII) [6] as photoreceptors, and proteorhodopsin (PR) [7] as another bacterial proton pump.

In each system the initial process is an ultrafast photoinduced cis-trans, resp. trans-cis isomerization of the retinal chromophore, covalently bound to the protein via a protonated Schiff base (Fig. 10.1). The reaction proceeds on the time scale of less than one up to several picoseconds and leads to a metastable state, thereby stabilizing the energy of the absorbed photon which is then used in a series of thermally driven reaction steps to accomplish the specific biological function on much longer time scales.

The task of this chapter is to give a status report about the results of ultrafast laser spectroscopy on the primary photoreaction in retinal proteins, their diversity, and their common features as well as related questions and challenges. For earlier related reviews the reader is referred to articles on retinal proteins [24–27], their primary photochemistry [28–31], and its modeling [20, 32].

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Diller, R. (2008). Primary Reactions in Retinal Proteins. In: Braun, M., Gilch, P., Zinth, W. (eds) Ultrashort Laser Pulses in Biology and Medicine. Biological and Medical Physics, Biomedical Engineering. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-73566-3_10

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