PMID: 9421960Jan 9, 1998Paper

Absorbance changes by aromatic amino acid side chains in early rhodopsin photointermediates

Photochemistry and Photobiology
J W LewisD S Kliger

Abstract

Absorbance changes were monitored from 250 to 650 nm during the first microsecond after photolysis of detergent suspensions of bovine rhodopsin at 20 degrees C. Global analysis of the resulting data produced difference spectra for bathorhodopsin, BSI and lumirhodopsin which give the change in absorbance of the aromatic amino acid side chains in these photointermediates relative to rhodopsin. These spectra show that the significant bleaching of absorbance near 280 nm, which has been seen previously for the lumirhodopsin, metarhodopsin I and metarhodopsin II intermediates, extends to times as early as bathorhodopsin. Because no corresponding absorbance increase is observed in the 250-275 nm region, the earliest bleaching of the 280 nm absorbance in rhodopsin is attributed to disruption of a hyperchromic interaction affecting Trp265. Partial decay of this 280 nm bleaching as bathorhodopsin converts to BSI takes place maximally near 290 nm, where Trp265 has been shown to absorb, and could be due to the ring of the retinylidene chromophore resuming a position at the BSI stage that reestablishes the hyperchromic interaction with Trp265. A subsequent change in the 250-300 nm region, which has no counterpart in the visible chromophore ...Continue Reading

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Citations

May 29, 2000·Biophysical Journal·S P BalashovN Kamo
Oct 3, 2001·Physiological Reviews·S T MenonT P Sakmar

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