Electric-field-induced Schiff-base deprotonation in D85N mutant bacteriorhodopsin

Paul Kolodner, Evgeniy P. Lukashev, Yuan Chin Ching, Denis L. Rousseau

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

The application of an external electric field to dry films of Asp-85 → Asn mutant bacteriorhodopsin causes deprotonation of the Schiff base, resulting in a shift of the optical absorption maximum from 600 nm to 400 nm. This is in marked contrast to the case of wild-type bacteriorhodopsin films, in which electric fields produce a red-shifted product whose optical properties are similar to those of the acid-blue form of the protein. This difference is due to the much weaker binding of the Schiff-base proton in the mutant protein, as indicated by its low pK of ≃9, as compared with the value pK ≃ 13 in the wild type. Other bacteriorhodopsins with lowered Schiff-base pK values should also exhibit a field-induced shift in the protonation equilibrium of the Schiff base. We propose mechanisms to account for these observations.

Original languageEnglish (US)
Pages (from-to)11618-11621
Number of pages4
JournalProceedings of the National Academy of Sciences of the United States of America
Volume93
Issue number21
DOIs
StatePublished - Oct 15 1996

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Bacteriorhodopsins
Schiff Bases
Mutant Proteins
Protons
Acids
Proteins

ASJC Scopus subject areas

  • Genetics
  • General

Cite this

Electric-field-induced Schiff-base deprotonation in D85N mutant bacteriorhodopsin. / Kolodner, Paul; Lukashev, Evgeniy P.; Ching, Yuan Chin; Rousseau, Denis L.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 93, No. 21, 15.10.1996, p. 11618-11621.

Research output: Contribution to journalArticle

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