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 Jjournal_title
Biophysical journalauthors
Milder SJdoi
10.1016/S0006-3495(91)82070-7subject
Has Abstractpub_date
1991-08-01 00:00:00pages
440-6issue
2eissn
0006-3495issn
1542-0086pii
S0006-3495(91)82070-7journal_volume
60pub_type
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