Influence of a chromophore analogue in the protein cage of a photoactive yellow protein
Author:
Affiliation:
1. Science & Technology Entrepreneurship Laboratory (e-square)
2. Osaka University
3. Suita
4. Japan
5. Department of Science
6. Toyonaka
Abstract
To understand the mechanism of photo-isomerization, photoactive yellow protein (PYP) containing cyano-p-coumaric acid (CHCA) were investigated.
Publisher
Springer Science and Business Media LLC
Subject
Physical and Theoretical Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2015/PP/C5PP00176E
Reference33 articles.
1. Isolation and characterization of soluble cytochromes, ferredoxins and other chromophoric proteins from the halophilic phototrophic bacterium Ectothiorhodospira halophila
2. The eubacterium Ectothiorhodospira halophila is negatively phototactic, with a wavelength dependence that fits the absorption spectrum of the photoactive yellow protein
3. Photoactive Yellow Protein, A New Type of Photoreceptor Protein: Will This “Yellow Lab” Bring Us Where We Want to Go?
4. Resonance Raman evidence that the thioester-linked 4-hydroxycinnamyl chromophore of photoactive yellow protein is deprotonated
5. Evidence fortrans-cisisomerization of thep-coumaric acid chromophore as the photochemical basis of the photocycle of photoactive yellow protein
Cited by 2 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. Structural and spectroscopic characterization of photoactive yellow protein and photoswitchable fluorescent protein constructs containing heavy atoms;Journal of Photochemistry and Photobiology A: Chemistry;2020-10
2. Role of Bulk Water Environment in Regulation of Functional Hydrogen-Bond Network in Photoactive Yellow Protein;The Journal of Physical Chemistry B;2015-12-10
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