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PHOTOCHEMICAL STUDIES OF ARTIFICIAL BACTERIORHODOPSINS
Author(s) -
Umadevi P.,
SHEVES M.,
Rosenbach V.,
Ottolenghi M.
Publication year - 1983
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1983.tb03862.x
Subject(s) - polyene , chemistry , bacteriorhodopsin , chromophore , moiety , ring (chemistry) , bicyclic molecule , stereochemistry , photochemistry , photoprotein , photodissociation , organic chemistry , membrane , biochemistry , calcium
— Three artificial bacteriorhodopsins are prepared [from synthetic aromatic and bicyclic analogues of retinal and exposed to spectroscopic and pulsed lader photolysis studies. The spectra of the pigments, all perturbed in the ring region of the molecule, are markedly blue shifted in respect to natural bacteriorhodopsin. The shift is attributed to a decreased effect of a protein charge in the vicinity of the ring, in agreement with the point‐charge model of Nakanishi et al. , 1980. The photocycles of the synthetic pigments exhibit a primary red‐shifted (K) intermediate and a blue shifted (M) transient, analogous to those observed for the natural pigment. Such observations impose considerable limitations, both on the possible chromophore conformational changes and on the effects of neighbouring protein charges associated with the photocycle. It is concluded that only the Schiff base counter‐ion, but not the ring charge, may be associated with the generation of the primary red shifted K species. Moreover, the rigidity imposed on the polyene by the additional ring in the bicyclic analogue shows that the photocycle can not be initiated by conformational changes in the retinyl moiety up to the C 9 carbon in the polyene chain. It is also observed that the K→L process in the photocycle is considerably slower in the case of the synthetic pigments. The observation is rationalized by attributing the process to a conformational change in the polyene moiety catalyzed by the ring protein charge.