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Hydrogen‐Bond Network Determines the Early Photoisomerization Processes of Cph1 and AnPixJ Phytochromes

Phytochrome proteins are light receptors that play a pivotal role in regulating the life cycles of plants and microorganisms. Intriguingly, while cyanobacterial phytochrome Cph1 and cyanobacteriochrome AnPixJ use the same phycocyanobilin (PCB) chromophore to absorb light, their excited‐state behavio...

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Autores principales: Liu, Xiang‐Yang, Zhang, Teng‐Shuo, Fang, Qiu, Fang, Wei‐Hai, González, Leticia, Cui, Ganglong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8456922/
https://www.ncbi.nlm.nih.gov/pubmed/34097335
http://dx.doi.org/10.1002/anie.202104853
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author Liu, Xiang‐Yang
Zhang, Teng‐Shuo
Fang, Qiu
Fang, Wei‐Hai
González, Leticia
Cui, Ganglong
author_facet Liu, Xiang‐Yang
Zhang, Teng‐Shuo
Fang, Qiu
Fang, Wei‐Hai
González, Leticia
Cui, Ganglong
author_sort Liu, Xiang‐Yang
collection PubMed
description Phytochrome proteins are light receptors that play a pivotal role in regulating the life cycles of plants and microorganisms. Intriguingly, while cyanobacterial phytochrome Cph1 and cyanobacteriochrome AnPixJ use the same phycocyanobilin (PCB) chromophore to absorb light, their excited‐state behavior is very different. We employ multiscale calculations to rationalize the different early photoisomerization mechanisms of PCB in Cph1 and AnPixJ. We found that their electronic S(1), T(1), and S(0) potential minima exhibit distinct geometric and electronic structures due to different hydrogen bond networks with the protein environment. These specific interactions influence the S(1) electronic structures along the photoisomerization paths, ultimately leading to internal conversion in Cph1 but intersystem crossing in AnPixJ. This explains why the excited‐state relaxation in AnPixJ is much slower (ca. 100 ns) than in Cph1 (ca. 30 ps). Further, we predict that efficient internal conversion in AnPixJ can be achieved upon protonating the carboxylic group that interacts with PCB.
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spelling pubmed-84569222021-09-27 Hydrogen‐Bond Network Determines the Early Photoisomerization Processes of Cph1 and AnPixJ Phytochromes Liu, Xiang‐Yang Zhang, Teng‐Shuo Fang, Qiu Fang, Wei‐Hai González, Leticia Cui, Ganglong Angew Chem Int Ed Engl Research Articles Phytochrome proteins are light receptors that play a pivotal role in regulating the life cycles of plants and microorganisms. Intriguingly, while cyanobacterial phytochrome Cph1 and cyanobacteriochrome AnPixJ use the same phycocyanobilin (PCB) chromophore to absorb light, their excited‐state behavior is very different. We employ multiscale calculations to rationalize the different early photoisomerization mechanisms of PCB in Cph1 and AnPixJ. We found that their electronic S(1), T(1), and S(0) potential minima exhibit distinct geometric and electronic structures due to different hydrogen bond networks with the protein environment. These specific interactions influence the S(1) electronic structures along the photoisomerization paths, ultimately leading to internal conversion in Cph1 but intersystem crossing in AnPixJ. This explains why the excited‐state relaxation in AnPixJ is much slower (ca. 100 ns) than in Cph1 (ca. 30 ps). Further, we predict that efficient internal conversion in AnPixJ can be achieved upon protonating the carboxylic group that interacts with PCB. John Wiley and Sons Inc. 2021-07-16 2021-08-16 /pmc/articles/PMC8456922/ /pubmed/34097335 http://dx.doi.org/10.1002/anie.202104853 Text en © 2021 The Authors. Angewandte Chemie International Edition published by Wiley-VCH GmbH https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Articles
Liu, Xiang‐Yang
Zhang, Teng‐Shuo
Fang, Qiu
Fang, Wei‐Hai
González, Leticia
Cui, Ganglong
Hydrogen‐Bond Network Determines the Early Photoisomerization Processes of Cph1 and AnPixJ Phytochromes
title Hydrogen‐Bond Network Determines the Early Photoisomerization Processes of Cph1 and AnPixJ Phytochromes
title_full Hydrogen‐Bond Network Determines the Early Photoisomerization Processes of Cph1 and AnPixJ Phytochromes
title_fullStr Hydrogen‐Bond Network Determines the Early Photoisomerization Processes of Cph1 and AnPixJ Phytochromes
title_full_unstemmed Hydrogen‐Bond Network Determines the Early Photoisomerization Processes of Cph1 and AnPixJ Phytochromes
title_short Hydrogen‐Bond Network Determines the Early Photoisomerization Processes of Cph1 and AnPixJ Phytochromes
title_sort hydrogen‐bond network determines the early photoisomerization processes of cph1 and anpixj phytochromes
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8456922/
https://www.ncbi.nlm.nih.gov/pubmed/34097335
http://dx.doi.org/10.1002/anie.202104853
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