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Literature DB >> 2756001

Kinetic model of bacteriorhodopsin photocycle: pathway from M state to bR.

D S Chernavskii, I V Chizhov, R H Lozier, T M Murina, A M Prokhorov, B V Zubov.

Abstract

A model of the last parts of the bacteriorhodopsin (bR) photocycle is proposed on the basis of experimental data for the kinetic behavior of the 'O' intermediate during a temperature pulse in distilled water suspension. The model includes the previously proposed (but not well characterized) intermediate 'N' between the 'M' and 'O' states of bR. This intermediate exists in fast temperature-dependent quasi-stationary equilibrium with the red-shifted intermediate 'O' and has a maximum of absorption close to the bR spectrum.

Entities: Chemical

Mesh：

Substances：
Bacteriorhodopsins

Year: 1989 PMID： 2756001 DOI： 10.1111/j.1751-1097.1989.tb08437.x

Source DB: PubMed Journal: Photochem Photobiol ISSN： 0031-8655 Impact factor: 3.421

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Cited

15 in total

1. On the protein residues that control the yield and kinetics of O(630) in the photocycle of bacteriorhodopsin.

Authors: Q Li; S Bressler; D Ovrutsky; M Ottolenghi; N Friedman; M Sheves
Journal: Biophys J Date: 2000-01 Impact factor: 4.033

2. Time-resolved step-scan Fourier transform infrared spectroscopy reveals differences between early and late M intermediates of bacteriorhodopsin.

Authors: C Rödig; I Chizhov; O Weidlich; F Siebert
Journal: Biophys J Date: 1999-05 Impact factor: 4.033

9. Deriving the intermediate spectra and photocycle kinetics from time-resolved difference spectra of bacteriorhodopsin. The simpler case of the recombinant D96N protein.

Authors: L Zimányi; J K Lanyi
Journal: Biophys J Date: 1993-01 Impact factor: 4.033

10. Simultaneous monitoring of light-induced changes in protein side-group protonation, chromophore isomerization, and backbone motion of bacteriorhodopsin by time-resolved Fourier-transform infrared spectroscopy.

Authors: K Gerwert; G Souvignier; B Hess
Journal: Proc Natl Acad Sci U S A Date: 1990-12-15 Impact factor: 11.205

Kinetic model of bacteriorhodopsin photocycle: pathway from M state to bR.

1. On the protein residues that control the yield and kinetics of O(630) in the photocycle of bacteriorhodopsin.

2. Time-resolved step-scan Fourier transform infrared spectroscopy reveals differences between early and late M intermediates of bacteriorhodopsin.

3. Proton uptake mechanism of bacteriorhodopsin as determined by time-resolved stroboscopic-FTIR-spectroscopy.

4. Nanosecond photolytic interruption of bacteriorhodopsin photocycle: K-590 --> BR-570 reaction.

5. Temperature and pH sensitivity of the O(640) intermediate of the bacteriorhodopsin photocycle.

6. Arginine-82 regulates the pKa of the group responsible for the light-driven proton release in bacteriorhodopsin.

7. Spectrally silent transitions in the bacteriorhodopsin photocycle.

8. pH-sensitive vibrational probe reveals a cytoplasmic protonated cluster in bacteriorhodopsin.

9. Deriving the intermediate spectra and photocycle kinetics from time-resolved difference spectra of bacteriorhodopsin. The simpler case of the recombinant D96N protein.

10. Simultaneous monitoring of light-induced changes in protein side-group protonation, chromophore isomerization, and backbone motion of bacteriorhodopsin by time-resolved Fourier-transform infrared spectroscopy.