Low-temperature retinal photoisomerization dynamics in bacteriorhodopsin

Article Abstract:

The excited state characteristics of bacteriorhodopsin (bR) was examined at a temperature of 20 femtosecond durations. bR decay at room temperature was measured with a lifetime of 0.5-ps while at 20 K, the decay was divided into two components, a dominant component of 0.5 ps and a minor component of 0.9-1.2 ps lifetime. The results indicate that retinal lifetime at physiological temperature is barrierless. The properties of the dominant and minor components of bR decay are analyzed in the context of low-temperature glass heterogeneity.

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Protein structural changes in bacteriorhodopsin upon photoisomerization as revealed by polarized FTIR spectroscopy

Article Abstract:

Infrared spectral changes between bacteriorhodopsin (BR) and the K-intermediate in the whole mid-infrared region were investigated using polarized Fourier transform infrared spectroscopy. Complete vibrational information was obtained on how the protein responds to the displacement of the chromophore. Changes in the oxygen-hydrogen and nitrogen-hydrogen stretching vibrations provided relevant frequencies on the bonding strength as well as the angles to the membrane normal.

Usage, Proteins, Protein structure, Fourier transform spectroscopy

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Quantitative determination of the protein catalytic efficiency for the retinal excited-state decay in bacteriorhodopsin

Article Abstract:

Pump-probe studies utilizing 100 fs laser pulses were used to quantitatively determine the protein catalysis for the key process in native bacteriorhodopsin by determining which decay component results from the excited state of the all-trans isomer. Findings showed that the ratio of the amplitudes of the two decay components in blue bacteriorhodopsin are affected by changes in the excitation wavelength.

Analysis, Bacterial proteins

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