Resonance Raman Evidence for Two Conformations Involved in the L Intermediate of Photoactive Yellow Protein
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference26 articles.
1. Isolation and characterization of soluble cytochromes, ferredoxins and other chromophoric proteins from the halophilic phototrophic bacterium Ectothiorhodospira halophila
2. Photoactive yellow protein: A structural prototype for the three-dimensional fold of the PAS domain superfamily
3. 1.4 .ANG. Structure of Photoactive Yellow Protein, a Cytosolic Photoreceptor: Unusual Fold, Active Site, and Chromophore
4. Resonance Raman evidence that the thioester-linked 4-hydroxycinnamyl chromophore of photoactive yellow protein is deprotonated
5. Dual Photoactive Species in Glu46Asp and Glu46Ala Mutants of Photoactive Yellow Protein: A pH-Driven Color Transition
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1. Reisomerization of retinal represents a molecular switch mediating Na+ uptake and release by a bacterial sodium-pumping rhodopsin;Journal of Biological Chemistry;2022-09
2. Femtosecond-to-millisecond mid-IR spectroscopy of photoactive yellow protein uncovers structural micro-transitions of the chromophore’s protonation mechanism;The Journal of Chemical Physics;2022-05-28
3. Probing Structure and Reaction Dynamics of Proteins Using Time-Resolved Resonance Raman Spectroscopy;Chemical Reviews;2019-12-09
4. Probing the early stages of photoreception in photoactive yellow protein with ultrafast time-domain Raman spectroscopy;Nature Chemistry;2017-02-06
5. Proton transfer reactions and hydrogen-bond networks in protein environments;Journal of The Royal Society Interface;2014-02-06
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