THE ‘OPSIN SHIFT’ IN BACTERIORHODOPSIN: STUDIES WITH ARTIFICIAL BACTERIORHODOPSINS

Valeria Balogh‐Nair, John D. Carriker, Barry Honig, Vinayak Kamat, Michael G. Motto, Koji Nakanishi, Ranjan Sen, Mordechai Sheves, Maria Arnaboldi Tanis, Kazuo Tsujimoto

Research output: Contribution to journalArticlepeer-review

Abstract

Abstract— The difference (in cm−1) in absorption maxima between the protonated Schiff base of retinals and the pigment derived therefrom has been defined as the opsin shift. It represents the influence of the opsin binding site on the chromophore. The analysis of the opsin shifts of a series of dihydrobacteriorhodopsins has led to the external point‐charge model, which in addition to a counter anion near the Schiff base ammonium, carries another negative charge in the vicinity of the β‐ionone ring. This is in striking contrast to the external point‐charge model proposed earlier for the bovine visual pigment. The absorption maxima of rhodopsins formed from bromo‐ and phenyl retinals support the two models. A retinal carrying a photoaffinity label has yielded a nonbleachable bacteriorhodopsin.

Original languageEnglish (US)
Pages (from-to)483-488
Number of pages6
JournalPhotochemistry and Photobiology
Volume33
Issue number4
DOIs
StatePublished - 1981
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Medicine(all)
  • Physical and Theoretical Chemistry

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