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Energy Transfer Dynamics in Light-Harvesting Complex 2 Variants Containing Oxidized B800 Bacteriochlorophyll a.
Saga, Yoshitaka; Otsuka, Yuji; Tanaka, Aiko; Masaoka, Yuto; Hidaka, Tsubasa; Nagasawa, Yutaka.
Afiliación
  • Saga Y; Department of Chemistry, Faculty of Science and Engineering, Kindai University, Higashi-Osaka, Osaka 577-8502, Japan.
  • Otsuka Y; Department of Chemistry, Faculty of Science and Engineering, Kindai University, Higashi-Osaka, Osaka 577-8502, Japan.
  • Tanaka A; Department of Chemistry, Faculty of Science and Engineering, Kindai University, Higashi-Osaka, Osaka 577-8502, Japan.
  • Masaoka Y; Graduate School of Life Sciences, Ritsumeikan University, Kusatsu, Shiga 525-8577, Japan.
  • Hidaka T; Graduate School of Life Sciences, Ritsumeikan University, Kusatsu, Shiga 525-8577, Japan.
  • Nagasawa Y; Graduate School of Life Sciences, Ritsumeikan University, Kusatsu, Shiga 525-8577, Japan.
J Phys Chem B ; 125(25): 6830-6836, 2021 07 01.
Article en En | MEDLINE | ID: mdl-34139847
Excitation energy transfer (EET) in light-harvesting proteins is vital for photosynthetic activities. The pigment compositions and their organizations in these proteins are responsible for the EET functions. Thus, changing the pigment compositions in light-harvesting proteins contributes to a better understanding of EET mechanisms. In this study, we investigated the EET dynamics of two light-harvesting complex 2 (LH2) variants, in which nine B800 bacteriochlorophyll (BChl) a pigments were entirely or half converted to 3-acetyl chlorophyll (AcChl) a. The AcChl a pigments showed a Qy band, which was blue-shifted by 107 nm from B800 BChl a in the two variants. EET from AcChl a to B850 BChl a was observed in both fully oxidized and half-oxidized LH2 variants, but the EET rates were lower than that from B800 to B850 BChl a. EET from AcChl a to the co-present B800 was barely detected in the half-oxidized LH2. The preferential EET from AcChl a to B850 instead of B800 was rationalized by little spectral overlap of AcChl a with B800 BChl a and the pigment geometry in the protein. The EET rate from B800 to B850 BChl a in the half-oxidized LH2 was analogous to that in native LH2, indicating that partial oxidation of B800 did not disturb the EET channel from the residual B800 to B850.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Bacterioclorofila A / Complejos de Proteína Captadores de Luz Idioma: En Revista: J Phys Chem B Asunto de la revista: QUIMICA Año: 2021 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Bacterioclorofila A / Complejos de Proteína Captadores de Luz Idioma: En Revista: J Phys Chem B Asunto de la revista: QUIMICA Año: 2021 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Estados Unidos