Hydrogen-Bonding Interaction Regulates Photoisomerization of a Single-Bond-Rotation Locked Photoactive Yellow Protein Chromophore in Protein-Reference-Cited by-同舟云学术

Hydrogen-Bonding Interaction Regulates Photoisomerization of a Single-Bond-Rotation Locked Photoactive Yellow Protein Chromophore in Protein

Published:2020-03-09 Issue:7 Volume:11 Page:2470-2476
ISSN:1948-7185
Container-title:The Journal of Physical Chemistry Letters
language:en
Short-container-title:J. Phys. Chem. Lett.

Author:

Zhang Teng-Shuo¹,Fang Ye-Guang¹,Song Xiu-Fang¹,Fang Wei-Hai¹^ORCID,Cui Ganglong¹^ORCID

Affiliation:

1. Key Laboratory of Theoretical and Computational Photochemistry, Ministry of Education, Chemistry College, Beijing Normal University, Beijing 100875, P.R. China

Funder

Ministry of Education of the People's Republic of China

National Natural Science Foundation of China

Publisher

American Chemical Society (ACS)

Subject

General Materials Science,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jpclett.0c00294

Reference51 articles.

1. Isolation and characterization of soluble cytochromes, ferredoxins and other chromophoric proteins from the halophilic phototrophic bacterium Ectothiorhodospira halophila

2. Photoactive yellow protein from the purple phototrophic bacterium, Ectothiorhodospira halophila. Quantum yield of photobleaching and effects of temperature, alcohols, glycerol, and sucrose on kinetics of photobleaching and recovery

3. Picosecond decay kinetics and quantum yield of fluorescence of the photoactive yellow protein from the halophilic purple phototrophic bacterium, Ectothiorhodospira halophila

4. The eubacterium Ectothiorhodospira halophila is negatively phototactic, with a wavelength dependence that fits the absorption spectrum of the photoactive yellow protein

5. Protein folding thermodynamics applied to the photocycle of the photoactive yellow protein

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