Low-temperature time-resolved spectroscopic study of the major light-harvesting complex of Amphidinium carterae

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F13%3A00425934" target="_blank" >RIV/60077344:_____/13:00425934 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60076658:12310/13:43885182

Výsledek na webu

<a href="http://dx.doi.org/10.1007/s11120-013-9900-8" target="_blank" >http://dx.doi.org/10.1007/s11120-013-9900-8</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s11120-013-9900-8" target="_blank" >10.1007/s11120-013-9900-8</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Low-temperature time-resolved spectroscopic study of the major light-harvesting complex of Amphidinium carterae

Popis výsledku v původním jazyce

The major light-harvesting complex of Amphidinium (A.) carterae, chlorophyll-a?chlorophyll-c 2?peridinin?protein complex (acpPC), was studied using ultrafast pump-probe spectroscopy at low temperature (60 K). An efficient peridinin?chlorophyll-a energy transfer was observed. The stimulated emission signal monitored in the near-infrared spectral region was stronger when redder part of peridinin pool was excited, indicating that these peridinins have the S1/ICT (intramolecular charge-transfer) state withsignificant charge-transfer character. This may lead to enhanced energy transfer efficiency from ?red peridinins to chlorophyll-a. Contrary to the water-soluble antenna of A. carterae, peridinin?chlorophyll-a protein, the energy transfer rates in acpPC were slower under low-temperature conditions. This fact underscores the influence of the protein environment on the excited-state dynamics of pigments and/or the specificity of organization of the two pigment?protein complexes.

Název v anglickém jazyce

Low-temperature time-resolved spectroscopic study of the major light-harvesting complex of Amphidinium carterae

Popis výsledku anglicky

The major light-harvesting complex of Amphidinium (A.) carterae, chlorophyll-a?chlorophyll-c 2?peridinin?protein complex (acpPC), was studied using ultrafast pump-probe spectroscopy at low temperature (60 K). An efficient peridinin?chlorophyll-a energy transfer was observed. The stimulated emission signal monitored in the near-infrared spectral region was stronger when redder part of peridinin pool was excited, indicating that these peridinins have the S1/ICT (intramolecular charge-transfer) state withsignificant charge-transfer character. This may lead to enhanced energy transfer efficiency from ?red peridinins to chlorophyll-a. Contrary to the water-soluble antenna of A. carterae, peridinin?chlorophyll-a protein, the energy transfer rates in acpPC were slower under low-temperature conditions. This fact underscores the influence of the protein environment on the excited-state dynamics of pigments and/or the specificity of organization of the two pigment?protein complexes.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

BO - Biofyzika

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2013

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Photosynthesis Research

ISSN

0166-8595

e-ISSN

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Svazek periodika

117

Číslo periodika v rámci svazku

1-3

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

9

Strana od-do

257-265

Kód UT WoS článku

000326604900018

EID výsledku v databázi Scopus

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