Effects of Modification of Protein Nanospace Structure and Change of Temperature on the Femtosecond to Picosecond Fluorescence Dynamics of Photoactive Yellow Protein
- 4 May 2000
- journal article
- research article
- Published by American Chemical Society (ACS) in The Journal of Physical Chemistry B
- Vol. 104 (21) , 5191-5199
- https://doi.org/10.1021/jp994205+
Abstract
No abstract availableKeywords
This publication has 32 references indexed in Scilit:
- Femtosecond Polarized Pump−Probe and Stimulated Emission Spectroscopy of the Isomerization Reaction of RhodopsinThe Journal of Physical Chemistry A, 1998
- Environmental Effects on the Femtosecond−Picosecond Fluorescence Dynamics of Photoactive Yellow Protein: Chromophores in Aqueous Solutions and in Protein Nanospaces Modified by Site-Directed MutagenesisThe Journal of Physical Chemistry B, 1998
- Rhodopsin Emission in Real Time: A New Aspect of the Primary Event in VisionJournal of the American Chemical Society, 1998
- Structure of a Protein Photocycle Intermediate by Millisecond Time-Resolved CrystallographyScience, 1997
- Evidence for trans‐cis isomerization of the p‐coumaric acid chromophore as the photochemical basis of the photocycle of photoactive yellow proteinFEBS Letters, 1996
- Photoreaction Cycle of Photoactive Yellow Protein from Ectothiorhodospira halophila Studied by Low-Temperature SpectroscopyBiochemistry, 1996
- Reconstitution photoactive yellow protein from apoprotein and p‐coumaric acid derivativesFEBS Letters, 1995
- Resonance Raman evidence that the thioester-linked 4-hydroxycinnamyl chromophore of photoactive yellow protein is deprotonatedBiochemistry, 1995
- Thiol ester-linked p-coumaric acid as a new photoactive prosthetic group in a protein with rhodopsin-like photochemistryBiochemistry, 1994
- Properties of a water-soluble, yellow protein isolated from a halophilic phototrophic bacterium that has photochemical activity analogous to sensory rhodopsinBiochemistry, 1987