Reorientation of the Retinylidene Chromophore in the K, L, and M Intermediates of Bacteriorhodopsin from Time-Resolved Linear Dichroism: Resolving Kinetically and Spectrally Overlapping Intermediates of Chromoproteins-Reference-Cited by-同舟云学术

Reorientation of the Retinylidene Chromophore in the K, L, and M Intermediates of Bacteriorhodopsin from Time-Resolved Linear Dichroism: Resolving Kinetically and Spectrally Overlapping Intermediates of Chromoproteins

Published:1999-07-01 Issue:30 Volume:103 Page:6371-6383
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Borucki Berthold¹,Otto Harald¹,Heyn Maarten P.¹

Affiliation:

1. Biophysics Group, Physics Department, Freie Universität Berlin, Arnimallee 14, D-14195 Berlin, Germany

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/jp990679x

Reference27 articles.

1. From Femtoseconds to Biology: Mechanism of Bacteriorhodopsin's Light-Driven Proton Pump

2. Chromophore structural changes in rhodopsin from nanoseconds to microseconds following pigment photolysis

3. Photomorphogenesis in Plants

4. Properties of a water-soluble, yellow protein isolated from a halophilic phototrophic bacterium that has photochemical activity analogous to sensory rhodopsin

5. Structure at 0.85 Å resolution of an early protein photocycle intermediate

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