Evidence for light-induced 13-cis, 14-s-cis isomerization in bacteriorhodopsin obtained by FTIR difference spectroscopy using isotopically labelled retinals.

The EMBO journal ·Vol. 5 ·No. 4 ·1986-04-00 ·Pages 805-11

Gerwert K, Siebert F

Abstract

We have obtained by Fourier transformed infra-red (FTIR)-spectroscopy BR-K, BR-L and BR-M difference spectra of bacteriorhodopsin regenerated with isotopically labelled retinals. Thereby, we are able to assign reliably the C(14)-C(15) and C=N stretching vibrations of the various intermediates. The lower C(14)-C(15) stretching vibration frequency in L as compared with 13-cis protonated Schiff base model compounds indicates a 13-cis, 14-s-cis configuration of the retinal in this species. The unusually low C=N stretching vibration in K at 1615 cm indicates less stabilization of the positive charge at the Schiff base by the protein environment. Based on these results, a mechanism is suggested by which the stored light energy is transformed into proton transfers.

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Gerwert K

Institut für Biophysik und Strahlenbiologie der Universität, Albertstrasse 23, D-7800 Freiburg i. Brsg., FRG.

Siebert F

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Article Info

Journal

The EMBO journal

Abbr.

EMBO J

ISSN

0261-4189

Published

1986-04-00

Pages

805-11

Language

English

Region

England

NLM ID

8208664

PMCID

PMC1166862

External Links

PubMed source PMC Full Text View journal details

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Evidence for light-induced 13-cis, 14-s-cis isomerization in bacteriorhodopsin obtained by FTIR difference spectroscopy using isotopically labelled retinals.

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