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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1981 Dec;78(12):7379–7382. doi: 10.1073/pnas.78.12.7379

Resonance Raman study of the primary photochemistry of bacteriorhodopsin.

J Pande, R H Callender, T G Ebrey
PMCID: PMC349270  PMID: 6950382

Abstract

Resonance Raman multicomponent spectra of the light-adapted form of bacteriorhodopsin, bRLA568, and its first photoproduct, K628, have been obtained at liquid nitrogen temperatures. The spectra of both bRLA568 and K628 could be obtained with the known sample compositions under our irradiating conditions and computer subtraction techniques. In agreement with previous results, we find that both bRLA568 and K628 contain chromophores linked to the apoprotein by protonated Schiff bases of retinal. Neither pigment form, suspended in H2O or 2H2O, compares closely to the spectral features of all-trans and 13-cis protonated and deuterated model chromophores, respectively. The data are consistent with other results, suggesting that a chromophore isomerization takes place in the bRLA568-to-K628 phototransition. However, the exact structure of the in situ chromophore would appear not to involve simple trans-to-13-cis structures found in solution.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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