Correlation between absorption maxima and thermal isomerization rates in bacteriorhodopsin.

Abstract:

:The reported rates of thermal 13-cis to all-trans isomerization of the protonated Schiff base of retinal (PSBR) in solution and in bacteriorhodopsin (BR) are shown to be correlated with the red shift in the absorption maximum of the chromophore, though the linear fit is different for BR and for a model PSBR in solution. Because the red shift in the absorption has been previously shown to be correlated with pi-electron delocalization in the chromophore, this suggests that the thermal isomerization rate is largely regulated by the amount of double bond character in the chromophore. Because the linear fit of isomerization rates with absorption maxima is different for BR and the model PSBR, specific interactions of the protein with the chromophore must also be a factor in determining thermal isomerization rates in BR. A model of the later steps in the photocycle of BR is presented in which the 13-cis to all-trans thermal isomerization occurs during the O intermediate.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Milder SJ

doi

10.1016/S0006-3495(91)82070-7

subject

Has Abstract

pub_date

1991-08-01 00:00:00

pages

440-6

issue

2

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(91)82070-7

journal_volume

60

pub_type

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