Tyrosine structural changes detected during the photoactivation of rhodopsin

Frank DeLange, Corné H.W. Klaassen, Stacie E. Wallace-Williams, Petra H.M. Bovee-Geurtst, Xiao Mei Liu, Willem J. DeGrip, Kenneth J. Rothschild*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

41 Citations (Scopus)
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We present the first Fourier transform infrared (FTIR) analysis of an isotope-labeled eukaryotic membrane protein. A combination of isotope labeling and FTIR difference spectroscopy was used to investigate the possible involvement of tyrosines in the photoactivation of rhodopsin (Rho). Rho → MII difference spectra were obtained at 10 °C for unlabeled recombinant Rho and isotope-labeled L-[ring-2H4]Tyr-Rho expressed in Spodoptera frugiperda cells grown on a stringent culture medium containing enriched L-[ring-2H4]Tyr and isolated using a His6 tag. A comparison of these difference spectra revealed reproducible changes in bands that correspond to tyrosine and tyrosinate vibrational modes. A similar pattern of tyrosine/tyrosinate bands has also been observed in the bR → M transition in bacteriorhodopsin, although the sign of the bands is reversed. In bacteriorhodopsin, these bands were assigned to Tyr-185, which along with Pro-186 in the F-helix, may form a hinge that facilitates α-helix movement.

Original languageEnglish
Pages (from-to)23735-23739
Number of pages5
JournalJournal of Biological Chemistry
Issue number37
Publication statusPublished - 11 Sept 1998
Externally publishedYes


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