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Analogies between halorhodopsin and bacteriorhodopsin
1Institute of Biophysics, Biological Research Center of the Hungarian Academy of Sciences, H-6701, Szeged, Hungary.
Biochimica Et Biophysica Acta
|September 14, 2000
Summary
Bacteriorhodopsin and halorhodopsin, both retinal proteins, share similar structures and photocycles despite pumping different ions. Their functions can be explained by the
Area of Science:
- Biochemistry
- Molecular Biology
- Biophysics
Background:
- Bacteriorhodopsin and halorhodopsin are light-activated ion pumps belonging to the retinal protein family.
- Both proteins feature seven transmembrane alpha helices surrounding a retinal binding pocket.
Purpose of the Study:
- To compare the structure, photocycle, and ion-transport mechanisms of bacteriorhodopsin and halorhodopsin.
- To elucidate the energetic and kinetic differences in their ion-pumping functions.
Main Methods:
- Time-resolved spectroscopy to determine intermediate spectra (K, L, N, O).
- Absorption kinetic measurements to analyze photocycle dynamics.
- Photoinduced transient electric signal measurements to characterize electrogenicity.
Main Results:
- Spectra of photocycle intermediates are highly similar between bacteriorhodopsin and halorhodopsin.
- Halorhodopsin's photocycle lacks the M intermediate and is dominated by L intermediate.
- Bacteriorhodopsin's photocycle is entropy-driven, while halorhodopsin's is enthalpy-driven.
Conclusions:
- The 'local access' model adequately describes the function of both bacteriorhodopsin and halorhodopsin.
- Ion specificity can be altered in these proteins, enabling conversion between proton and chloride pumps.