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The role of charge-transfer states in energy transfer and dissipation within natural and artificial bacteriochlorophyll-proteins
Understanding how specific protein environments affect the mechanisms of non-radiative energy dissipation within densely assembled chlorophylls in photosynthetic protein complexes is of great interest to the construction of bioinspired solar energy conversion devices. Mixing of charge-transfer and e...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4255223/ https://www.ncbi.nlm.nih.gov/pubmed/25342121 http://dx.doi.org/10.1038/ncomms6287 |
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author | Wahadoszamen, Md. Margalit, Iris Ara, Anjue Mane van Grondelle, Rienk Noy, Dror |
author_facet | Wahadoszamen, Md. Margalit, Iris Ara, Anjue Mane van Grondelle, Rienk Noy, Dror |
author_sort | Wahadoszamen, Md. |
collection | PubMed |
description | Understanding how specific protein environments affect the mechanisms of non-radiative energy dissipation within densely assembled chlorophylls in photosynthetic protein complexes is of great interest to the construction of bioinspired solar energy conversion devices. Mixing of charge-transfer and excitonic states in excitonically interacting chlorophylls was implicated in shortening excited states lifetimes but its relevance to active control of energy dissipation in natural systems is under considerable debate. Here we show that the degree of fluorescence quenching in two similar pairs of excitonically interacting bacteriochlorophyll derivatives is directly associated with increasing charge transfer character in the excited state, and that the protein environment may control non-radiative dissipation by affecting the mixing of charge transfer and excitonic states. The capability of local protein environments to determine the fate of excited states, and thereby to confer different functionalities to excitonically coupled dimers substantiates the dimer as the basic functional element of photosynthetic enzymes. |
format | Online Article Text |
id | pubmed-4255223 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
record_format | MEDLINE/PubMed |
spelling | pubmed-42552232015-04-24 The role of charge-transfer states in energy transfer and dissipation within natural and artificial bacteriochlorophyll-proteins Wahadoszamen, Md. Margalit, Iris Ara, Anjue Mane van Grondelle, Rienk Noy, Dror Nat Commun Article Understanding how specific protein environments affect the mechanisms of non-radiative energy dissipation within densely assembled chlorophylls in photosynthetic protein complexes is of great interest to the construction of bioinspired solar energy conversion devices. Mixing of charge-transfer and excitonic states in excitonically interacting chlorophylls was implicated in shortening excited states lifetimes but its relevance to active control of energy dissipation in natural systems is under considerable debate. Here we show that the degree of fluorescence quenching in two similar pairs of excitonically interacting bacteriochlorophyll derivatives is directly associated with increasing charge transfer character in the excited state, and that the protein environment may control non-radiative dissipation by affecting the mixing of charge transfer and excitonic states. The capability of local protein environments to determine the fate of excited states, and thereby to confer different functionalities to excitonically coupled dimers substantiates the dimer as the basic functional element of photosynthetic enzymes. 2014-10-24 /pmc/articles/PMC4255223/ /pubmed/25342121 http://dx.doi.org/10.1038/ncomms6287 Text en Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms |
spellingShingle | Article Wahadoszamen, Md. Margalit, Iris Ara, Anjue Mane van Grondelle, Rienk Noy, Dror The role of charge-transfer states in energy transfer and dissipation within natural and artificial bacteriochlorophyll-proteins |
title | The role of charge-transfer states in energy transfer and dissipation within natural and artificial bacteriochlorophyll-proteins |
title_full | The role of charge-transfer states in energy transfer and dissipation within natural and artificial bacteriochlorophyll-proteins |
title_fullStr | The role of charge-transfer states in energy transfer and dissipation within natural and artificial bacteriochlorophyll-proteins |
title_full_unstemmed | The role of charge-transfer states in energy transfer and dissipation within natural and artificial bacteriochlorophyll-proteins |
title_short | The role of charge-transfer states in energy transfer and dissipation within natural and artificial bacteriochlorophyll-proteins |
title_sort | role of charge-transfer states in energy transfer and dissipation within natural and artificial bacteriochlorophyll-proteins |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4255223/ https://www.ncbi.nlm.nih.gov/pubmed/25342121 http://dx.doi.org/10.1038/ncomms6287 |
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