Literature DB >> 2540498

Dependency of photon density on primary process of cattle rhodopsin.

H Kandori, S Matuoka, Y Shichida, T Yoshizawa.   

Abstract

The primary photochemical reactions of cattle rhodopsin suspended in H2O or D2O were compared between excitation with both a weak and an intense picosecond laser pulse (wavelength, 532 nm; duration, 25 ps) at room temperature. The time-dependent change of absorbance at about 575 nm demonstrated that photohodopsin, a precursor of bathorhodopsin, was produced immediately after the excitation with a weak picosecond laser pulse. It decayed to bathorhodopsin with a time constant of 45 ps which is close to the value reported previously [Shichida et al., (1984) Photobiochem. Photobiophys., 7, 221-228]. No deuterium effect was observed in this process. Excitation with an intense laser pulse induced instantaneous increase of the absorbance at about 575 nm and remained at almost constant level on the picosecond time scale, which was in good agreement with the pioneering work [Busch et al., (1972) Proc. Natl. Acad. Sci., USA, 69, 2802-2806]. No deuterium effect was observed in this photochemical process.

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Year:  1989        PMID: 2540498     DOI: 10.1111/j.1751-1097.1989.tb04094.x

Source DB:  PubMed          Journal:  Photochem Photobiol        ISSN: 0031-8655            Impact factor:   3.421


  7 in total

Review 1.  Photointermediates of visual pigments.

Authors:  J W Lewis; D S Kliger
Journal:  J Bioenerg Biomembr       Date:  1992-04       Impact factor: 2.945

2.  Bathoiodopsin, a primary intermediate of iodopsin at physiological temperature.

Authors:  H Kandori; T Mizukami; T Okada; Y Imamoto; Y Fukada; Y Shichida; T Yoshizawa
Journal:  Proc Natl Acad Sci U S A       Date:  1990-11       Impact factor: 11.205

3.  Ultrafast spectroscopy of the visual pigment rhodopsin.

Authors:  M Yan; D Manor; G Weng; H Chao; L Rothberg; T M Jedju; R R Alfano; R H Callender
Journal:  Proc Natl Acad Sci U S A       Date:  1991-11-01       Impact factor: 11.205

4.  Absolute absorption spectra of batho- and photorhodopsins at room temperature. Picosecond laser photolysis of rhodopsin in polyacrylamide.

Authors:  H Kandori; Y Shichida; T Yoshizawa
Journal:  Biophys J       Date:  1989-09       Impact factor: 4.033

5.  Bathorhodopsin structure in the room-temperature rhodopsin photosequence: picosecond time-resolved coherent anti-Stokes Raman scattering.

Authors:  A Popp; L Ujj; G H Atkinson
Journal:  Proc Natl Acad Sci U S A       Date:  1996-01-09       Impact factor: 11.205

6.  Structure, initial excited-state relaxation, and energy storage of rhodopsin resolved at the multiconfigurational perturbation theory level.

Authors:  Tadeusz Andruniów; Nicolas Ferré; Massimo Olivucci
Journal:  Proc Natl Acad Sci U S A       Date:  2004-12-16       Impact factor: 11.205

7.  Photoisomerization mechanism of the rhodopsin chromophore: picosecond photolysis of pigment containing 11-cis-locked eight-membered ring retinal.

Authors:  T Mizukami; H Kandori; Y Shichida; A H Chen; F Derguini; C G Caldwell; C F Biffe; K Nakanishi; T Yoshizawa
Journal:  Proc Natl Acad Sci U S A       Date:  1993-05-01       Impact factor: 11.205

  7 in total

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