Photoproducts of bacteriorhodopsin mutants: a molecular dynamics study.

Abstract:

:Molecular dynamics simulations of wild-type bacteriorhodopsin (bR) and of its D85N, D85T, D212N, and Y57F mutants have been carried out to investigate possible differences in the photoproducts of these proteins. For each mutant, a series of 50 molecular dynamics simulations of the photoisomerization and subsequent relaxation process were completed. The photoproducts can be classified into four distinct classes: 1) 13-cis retinal, with the retinal N-H+ bond oriented toward Asp-96; 2) 13-cis retinal, with the N-H+ oriented toward Asp-85 and hydrogen-bonded to a water molecule; 3) 13,14-di-cis retinal; 4) all-trans retinal. Simulations of wild-type bR and of its Y57F mutant resulted mainly in class 1 and class 2 products; simulations of D85N, D85T, and D212N mutants resulted almost entirely in class 1 products. The results support the suggestion that only class 2 products initiate a functional pump cycle. The formation of class 1 products for the D85N, D85T, and D212N mutants can explain the reversal of proton pumping under illumination by blue and yellow light.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Humphrey W,Bamberg E,Schulten K

doi

10.1016/S0006-3495(97)78781-2

subject

Has Abstract

pub_date

1997-03-01 00:00:00

pages

1347-56

issue

3

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(97)78781-2

journal_volume

72

pub_type

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