Pigment structure in the FCP-like light-harvesting complex from Chromera velia

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F16%3A43890666" target="_blank" >RIV/60076658:12310/16:43890666 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60077344:_____/16:00464744

Výsledek na webu

<a href="http://www.sciencedirect.com/science/article/pii/S0005272816306065" target="_blank" >http://www.sciencedirect.com/science/article/pii/S0005272816306065</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.bbabio.2016.08.006" target="_blank" >10.1016/j.bbabio.2016.08.006</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Pigment structure in the FCP-like light-harvesting complex from Chromera velia

Popis výsledku v původním jazyce

Resonance Raman spectroscopy was used to evaluate pigment structure in the FCP-like light-harvesting complex of Chromera velia (Chromera light-harvesting complex or CLH). This antenna protein contains chlorophyll a, violaxanthin and a new isofucoxanthin-like carotenoid (called Ifx-l). We show that Ifx-l is present in two non-equivalent binding pockets with different conformations, having their (0,0) absorption maxima at 515 and 548 nm respectively. In this complex, only one violaxanthin population absorbing at 486 nm is observed. All the CLH-bound carotenoid molecules are in all-trans configuration, and among the two Ifx-l carotenoid molecules, the red one is twisted, as is the red-absorbing lutein in LHCII trimers. Analysis of the carbonyl stretching region for Chl a excitations indicates CLH binds up to seven Chl a molecules in five non-equivalent binding sites, in reasonable agreement with sequence analyses which have identified eight potential coordinating residues. The binding modes and conformations of CLH-bound pigments are discussed with respect to the known structures of LHCII and FCP.

Název v anglickém jazyce

Pigment structure in the FCP-like light-harvesting complex from Chromera velia

Popis výsledku anglicky

Resonance Raman spectroscopy was used to evaluate pigment structure in the FCP-like light-harvesting complex of Chromera velia (Chromera light-harvesting complex or CLH). This antenna protein contains chlorophyll a, violaxanthin and a new isofucoxanthin-like carotenoid (called Ifx-l). We show that Ifx-l is present in two non-equivalent binding pockets with different conformations, having their (0,0) absorption maxima at 515 and 548 nm respectively. In this complex, only one violaxanthin population absorbing at 486 nm is observed. All the CLH-bound carotenoid molecules are in all-trans configuration, and among the two Ifx-l carotenoid molecules, the red one is twisted, as is the red-absorbing lutein in LHCII trimers. Analysis of the carbonyl stretching region for Chl a excitations indicates CLH binds up to seven Chl a molecules in five non-equivalent binding sites, in reasonable agreement with sequence analyses which have identified eight potential coordinating residues. The binding modes and conformations of CLH-bound pigments are discussed with respect to the known structures of LHCII and FCP.

Druh

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

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

<a href="/cs/project/GBP501%2F12%2FG055" target="_blank" >GBP501/12/G055: Centrum fotosyntetického výzkumu</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2016

Kód důvěrnosti údajů

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

Název periodika

Biochimica et Biophysica Acta - Bioenergetics

ISSN

0005-2728

e-ISSN

—

Svazek periodika

1857

Číslo periodika v rámci svazku

11

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

7

Strana od-do

1759-1765

Kód UT WoS článku

000384867400005

EID výsledku v databázi Scopus

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