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13 cis trans photoisomerization of the bacteriorhodopsin chromophore under high light intensities


13 cis trans photoisomerization of the bacteriorhodopsin chromophore under high light intensities



Biologicheskie Membrany 3(10): 984-992



ISSN/ISBN: 0233-4755

The pathways and intermediates of light-adaptation of purple membranes (transformatin of 13-cis- to trans-bacteriorhodopsin) at high light intensities was studied by the low-temperature absorption spectroscopy. It was found that under these conditions light-adaptation proceeds not through dark transformation of the bathoproduct of 13-cis-bacteriorhodopsin, Kc, as at low light intensities, but through a new state, designated P582. The absorption spectrum of P582 is similar to that of trans-bacteriorhodopsin, but is 4 nm shifted to the longer wavelength. The quantum yield of P582 formation at -180.degree. C is about 3 .cntdot. 10-4, that is 3 order of magnitude lower than the yield of Kc. Illumination at .lambda. = 520 nm transforms up to 85% of 13-cis-bacteriorhodopsin into P582-intermediate at -180.degree. C. At temperatures -60.degree. C and higher P582 spontaneously converts into trans-bacteriorhodopsin. P582 is photoactive. Under illumination it transforms with the quantum efficiency of 0.1 into a bathoform which is analogous to K-form of trans-bacteriorhodopsin. This bathoform relaxes through L and M intermediates into trans-bacteriorhodopsin. The similarity of spectral and photochemical properties of p582 and trans-bacteriorhodopsin evidences for trans-configuration of retinal in the P582-state. The existence of P582 intermediate testifies to conformational differences in the protein environment of the chromophore in 13-cis- vs. trans-bacteriorhodopsin.

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Accession: 004532333

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