Between the ground- and M-state of bacteriorhodopsin the retinal transition dipole moment tilts out of the plane of the membrane by only 3 degrees.

Abstract:

:The orientation of the transition dipole moments in the ground state and the M-intermediate of bacteriorhodopsin were determined by time-resolved and steady-state polarized absorption spectroscopy on samples of oriented immobilized purple membranes. The angle between the transition dipole moment and the membrane normal decreases from 66.8 +/- 0.5 degrees in the all-trans ground state to 64.1 +/- 0.8 degrees in the 13-cis M-state. The light-induced isomerization of the chromophore is thus accompanied by an orientational change of only about 3 degrees out of the plane of the membrane. The absorption anisotropy at 410 nm remains constant over more than 4 decades of time covering both the rise and decay of M. Conformational changes accompanying a sequential M1----M2 transition thus do not affect the chromophore orientation.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Otto H,Heyn MP

doi

10.1016/0014-5793(91)81163-3

subject

Has Abstract

pub_date

1991-11-18 00:00:00

pages

111-4

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(91)81163-3

journal_volume

293

pub_type

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