Protonation state of Asp (Glu)-85 regulates the purple-to-blue transition in bacteriorhodopsin mutants Arg-82----Ala and Asp-85----Glu: the blue form is inactive in proton translocation.

doi:10.1073/pnas.87.3.1013

Article

Protonation state of Asp (Glu)-85 regulates the purple-to-blue transition in bacteriorhodopsin mutants Arg-82----Ala and Asp-85----Glu: the blue form is inactive in proton translocation.

Proceedings of the National Academy of Sciences of the United States of America - 1 Feb 1990

Subramaniam S, Marti T, Khorana H G

Abstract excerpt

Previous studies with site-specific mutants of bacteriorhodopsin have demonstrated that replacement of Asp-85 or Arg-82 affects the absorption spectrum. Between pH 5.5 and 7, the Asp-85----Glu and Arg-82----Ala mutants exist in a pH-dependent equilibrium between purple (lambda max approximately 5...

Topics

Alanine
Arginine
Aspartic Acid
Bacteriorhodopsins
Glutamates
Glutamic Acid
Halobacterium
Kinetics
Mutation
Protons
Spectrophotometry

Protonation state of Asp (Glu)-85 regulates the purple-to-blue transition in bacteriorhodopsin mutants Arg-82----Ala and Asp-85----Glu: the blue form is inactive in proton translocation.

Abstract excerpt

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