A PYP chromophore acts as a ‘photoacid’ in an isolated hydrogen bonded complex
Author:
Affiliation:
1. Department of Physics and Astronomy
2. Aarhus University
3. Denmark
4. Department of Chemistry
5. M. V. Lomonosov Moscow State University
Abstract
The light-induced response of a neutral photoactive yellow protein chromophore in a hydrogen-bonded complex with a proton acceptor has been studied by dual-detection action absorption spectroscopy and density functional theory.
Funder
Carlsbergfondet
Villum Fonden
Russian Foundation for Basic Research
Publisher
Royal Society of Chemistry (RSC)
Subject
Physical and Theoretical Chemistry,General Physics and Astronomy
Link
http://pubs.rsc.org/en/content/articlepdf/2016/CP/C6CP00433D
Reference27 articles.
1. Isolation and characterization of soluble cytochromes, ferredoxins and other chromophoric proteins from the halophilic phototrophic bacterium Ectothiorhodospira halophila
2. Primary structure of a photoactive yellow protein from the phototrophic bacteriumEctothiorhodospira halophila, with evidence for the mass and the binding site of the chromophore
3. Complete Chemical Structure of Photoactive Yellow Protein: Novel Thioester-Linked 4-Hydroxycinnamyl Chromophore and Photocycle Chemistry
4. Density Functional Study of the Photoactive Yellow Protein's Chromophore
5. Electronic structure of the photoactive yellow protein chromophore: Ab initio study of the low-lying excited singlet states
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