TY - JOUR
T1 - KINETIC ANALYSIS OF TIME‐RESOLVED INFRARED DIFFERENCE SPECTRA OF THE L and M INTERMEDIATES OF BACTERIORHODOPSIN
AU - Chen, Wei‐Ge ‐G
AU - Braiman, Mark S.
PY - 1991/12
Y1 - 1991/12
N2 - Abstract– Infrared difference spectra with 4 cm−1 spectral resolution and 10‐u.s temporal resolution, obtained previously with a stroboscopic Fourier‐transform difference technique (Braiman et al., 1991, Proc. Natl. Acad. Sci. USA 88, 2388), were analyzed by means of a global exponential fitting procedure based on singular value decomposition. Using a simple linear kinetic model K → L → M for the bacteriorhodopsin (bR) photocycle in the time range10–1000 μ.s at 16.5°C, it was possible to generate bR → L and bR → M difference spectra with signal/noise ratios comparable to those obtainable with low temperature difference spectroscopy. The resulting time‐resolved bR → L and bR‐→ M difference spectra are both very similar to the corresponding static FTIR difference spectra obtained at 175 K and 250 K, respectively. In the bR → L spectrum, however, there are interesting differences that may indicate a greater degree of deprotonation of Asp‐96 when L is formed at physiological temperatures than when it is observed in a low‐temperature steady state.
AB - Abstract– Infrared difference spectra with 4 cm−1 spectral resolution and 10‐u.s temporal resolution, obtained previously with a stroboscopic Fourier‐transform difference technique (Braiman et al., 1991, Proc. Natl. Acad. Sci. USA 88, 2388), were analyzed by means of a global exponential fitting procedure based on singular value decomposition. Using a simple linear kinetic model K → L → M for the bacteriorhodopsin (bR) photocycle in the time range10–1000 μ.s at 16.5°C, it was possible to generate bR → L and bR → M difference spectra with signal/noise ratios comparable to those obtainable with low temperature difference spectroscopy. The resulting time‐resolved bR → L and bR‐→ M difference spectra are both very similar to the corresponding static FTIR difference spectra obtained at 175 K and 250 K, respectively. In the bR → L spectrum, however, there are interesting differences that may indicate a greater degree of deprotonation of Asp‐96 when L is formed at physiological temperatures than when it is observed in a low‐temperature steady state.
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U2 - 10.1111/j.1751-1097.1991.tb02110.x
DO - 10.1111/j.1751-1097.1991.tb02110.x
M3 - Article
AN - SCOPUS:84989730159
SN - 0031-8655
VL - 54
SP - 905
EP - 910
JO - Photochemistry and photobiology
JF - Photochemistry and photobiology
IS - 6
ER -