Energy Transfer from Tryptophane Amino Acid Residues to Retinal in a Bacteriorhodopsin Molecule Within a Femtosecond Timescale

Overview

Journal Dokl Biochem Biophys

Specialties Biochemistry
Biophysics

Date 2002 Apr 10

PMID 11938670

Authors

O A Dzhemesyuk

S A Antipin

F E Gostev

I B Fedorovich

O M Sarkisov

M A Ostrovskii

Affiliations

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References

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Jang D, El-Sayed M . Tryptophan fluorescence quenching as a monitor for the protein conformation changes occurring during the photocycle of bacteriorhodopsin under different perturbations. Proc Natl Acad Sci U S A. 1989; 86(15):5815-9. PMC: 297721. DOI: 10.1073/pnas.86.15.5815. View

Haupts U, Tittor J, Oesterhelt D . Closing in on bacteriorhodopsin: progress in understanding the molecule. Annu Rev Biophys Biomol Struct. 1999; 28:367-99. DOI: 10.1146/annurev.biophys.28.1.367. View

Birge R . Nature of the primary photochemical events in rhodopsin and bacteriorhodopsin. Biochim Biophys Acta. 1990; 1016(3):293-327. DOI: 10.1016/0005-2728(90)90163-x. View

Oesterhelt D, Stoeckenius W . Rhodopsin-like protein from the purple membrane of Halobacterium halobium. Nat New Biol. 1971; 233(39):149-52. DOI: 10.1038/newbio233149a0. View