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Engineering Excitonically-Coupled Dimers in an Artificial Protein for Light Harvesting via Computational Modelling

  • Datos identificativos

    Identificador: imarina:9291544
    Autores:
    Curti, MMaffeis, VDuarte, LGTAShareef, SHallado, LXCurutchet, CRomero, E
    Resumen:
    In photosynthesis, pigment - protein complexes achieve outstanding photoinduced charge separation efficiencies through a set of strategies in which excited states delocalisation over multiple pigments ('excitons') and charge-transfer states play key roles. These concepts, and their implementation in bioinspired artificial systems, are attracting increasing attention due to the vast potential that could be tapped by realising efficient photochemical reactions. In particular, de novo designed proteins provide a diverse structural toolbox that can be used to manipulate the geometric and electronic properties of bound chromophore molecules. However, achieving excitonic and charge-transfer states requires closely spaced chromophores, a non-trivial aspect since a strong binding with the protein matrix needs to be maintained. Here, we show how a general-purpose artificial protein can be optimised via molecular dynamics simulations to improve its binding capacity of a chlorophyll derivative, achieving complexes in which chromophores form two closely spaced and strongly interacting dimers. Based on spectroscopy results and computational modelling, we demonstrate each dimer is excitonically coupled, and propose they display signatures of charge-transfer state mixing. This work could open new avenues for the rational design of chromophore - protein complexes with advanced functionalities. This article is protected by copyright. All rights reserved.© 2023 The Protein Society.
  • Otros:

    Autor según el artículo: Curti, M; Maffeis, V; Duarte, LGTA; Shareef, S; Hallado, LX; Curutchet, C; Romero, E
    Departamento: Química Física i Inorgànica
    Autor/es de la URV: Hallado Abaunza, Luisa Xiomara / Shareef, Saeed
    Palabras clave: Molecular-dynamics simulations Molecular dynamics De novo protein design Cofactor binding Artificial photosynthesis states stability spectroscopy molecular dynamics energy-transfer de-novo design de novo protein design complex ii cofactor binding
    Resumen: In photosynthesis, pigment - protein complexes achieve outstanding photoinduced charge separation efficiencies through a set of strategies in which excited states delocalisation over multiple pigments ('excitons') and charge-transfer states play key roles. These concepts, and their implementation in bioinspired artificial systems, are attracting increasing attention due to the vast potential that could be tapped by realising efficient photochemical reactions. In particular, de novo designed proteins provide a diverse structural toolbox that can be used to manipulate the geometric and electronic properties of bound chromophore molecules. However, achieving excitonic and charge-transfer states requires closely spaced chromophores, a non-trivial aspect since a strong binding with the protein matrix needs to be maintained. Here, we show how a general-purpose artificial protein can be optimised via molecular dynamics simulations to improve its binding capacity of a chlorophyll derivative, achieving complexes in which chromophores form two closely spaced and strongly interacting dimers. Based on spectroscopy results and computational modelling, we demonstrate each dimer is excitonically coupled, and propose they display signatures of charge-transfer state mixing. This work could open new avenues for the rational design of chromophore - protein complexes with advanced functionalities. This article is protected by copyright. All rights reserved.© 2023 The Protein Society.
    Áreas temáticas: Química Molecular biology Medicine (miscellaneous) Interdisciplinar Farmacia Ciências biológicas iii Ciências biológicas ii Ciências biológicas i Biotecnología Biochemistry & molecular biology Biochemistry
    Acceso a la licencia de uso: https://creativecommons.org/licenses/by/3.0/es/
    Direcció de correo del autor: luisaxiomara.hallado@estudiants.urv.cat saeed.shareef@estudiants.urv.cat
    Identificador del autor: 0000-0002-8412-1939
    Fecha de alta del registro: 2024-08-03
    Versión del articulo depositado: info:eu-repo/semantics/publishedVersion
    Enlace a la fuente original: https://onlinelibrary.wiley.com/doi/full/10.1002/pro.4579
    URL Documento de licencia: https://repositori.urv.cat/ca/proteccio-de-dades/
    Referencia al articulo segun fuente origial: Protein Science. 32 (3): e4579-e4579
    Referencia de l'ítem segons les normes APA: Curti, M; Maffeis, V; Duarte, LGTA; Shareef, S; Hallado, LX; Curutchet, C; Romero, E (2023). Engineering Excitonically-Coupled Dimers in an Artificial Protein for Light Harvesting via Computational Modelling. Protein Science, 32(3), e4579-e4579. DOI: 10.1002/pro.4579
    DOI del artículo: 10.1002/pro.4579
    Entidad: Universitat Rovira i Virgili
    Año de publicación de la revista: 2023
    Tipo de publicación: Journal Publications
  • Palabras clave:

    Biochemistry,Biochemistry & Molecular Biology,Medicine (Miscellaneous),Molecular Biology
    Molecular-dynamics simulations
    Molecular dynamics
    De novo protein design
    Cofactor binding
    Artificial photosynthesis
    states
    stability
    spectroscopy
    molecular dynamics
    energy-transfer
    de-novo design
    de novo protein design
    complex ii
    cofactor binding
    Química
    Molecular biology
    Medicine (miscellaneous)
    Interdisciplinar
    Farmacia
    Ciências biológicas iii
    Ciências biológicas ii
    Ciências biológicas i
    Biotecnología
    Biochemistry & molecular biology
    Biochemistry
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