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On the two forms of bacteriorhodopsin

Komrakov AYu1, A D Kaulen

  • 1A.N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Russian Federation.

FEBS Letters
|March 7, 1994
PubMed
Summary

Bacteriorhodopsin

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Formation of the M(N) (M(open)) intermediate in the wild-type bacteriorhodopsin photocycle is accompanied by an absorption spectrum shift to shorter wavelength, like that in the mutant D96N bacteriorhodopsin photocycle.

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Area of Science:

  • Biophysics
  • Photochemistry
  • Protein Dynamics

Background:

  • Previous studies identified two components in wild-type bacteriorhodopsin's M-intermediate formation.
  • These components, with distinct time constants, suggested independent formation pathways.

Purpose of the Study:

  • Investigate M-intermediate formation in the D115N bacteriorhodopsin mutant.
  • Characterize the influence of pH and alkaline incubation on bacteriorhodopsin's photocycle dynamics.

Main Methods:

  • Spectroscopic analysis of M-intermediate formation kinetics.
  • pH-dependent measurements and long-term alkaline incubation of bacteriorhodopsin mutants.

Main Results:

  • The D115N mutant exhibited a 1:1 ratio of fast and slow M-intermediate formation components.
  • The slow phase disappeared below pH 6.2, leaving only the fast component.
  • Alkaline incubation induced an irreversible transformation to a non-photocyclic bR460 form, retaining only the fast M-intermediate.

Conclusions:

  • Bacteriorhodopsin exists in two spectroscopically similar forms at neutral pH, distinguished by their M-intermediate formation kinetics.
  • The D115N mutation alters the contribution ratio of these formation pathways.
  • The bR460 form represents a non-photocyclic state of bacteriorhodopsin.

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