Twisting a beta-Carotene, an Adaptive Trick from Nature for Dissipating Energy during Photoprotection

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F17%3A43895561" target="_blank" >RIV/60076658:12310/17:43895561 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61388971:_____/17:00473562

Výsledek na webu

<a href="http://www.jbc.org/content/292/4/1396" target="_blank" >http://www.jbc.org/content/292/4/1396</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1074/jbc.M116.753723" target="_blank" >10.1074/jbc.M116.753723</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Twisting a beta-Carotene, an Adaptive Trick from Nature for Dissipating Energy during Photoprotection

Popis výsledku v původním jazyce

Cyanobacteria possess a family of one-helix high light-inducible proteins (Hlips) that are homologous to light-harvesting antenna of plants and algae. An Hlip protein, high light-inducible protein D (HliD) purified as a small complex with the Ycf39 protein is evaluated using resonance Raman spectroscopy. We show that the HliD binds two different beta-carotenes, each present in two non-equivalent binding pockets with different conformations, having their (0,0) absorption maxima at 489 and 522 nm, respectively. Both populations of beta-carotene molecules were in all-trans configuration and the absorption position of the farthest blue-shifted beta-carotene was attributed entirely to the polarizability of the environment in its binding pocket. In contrast, the absorption maximum of the red-shifted beta-carotene was attributed to two different factors: the polarizability of the environment in its binding pocket and, more importantly, to the conformation of its beta-rings. This second beta-carotene has highly twisted beta-rings adopting a flat conformation, which implies that the effective conjugation length N is extended up to 10.5 modifying the energetic levels. This increase in N will also result in a lower S-1 energy state, which may provide a permanent energy dissipation channel. Analysis of the carbonyl stretching region for chlorophyll a excitations indicates that the HliD binds six chlorophyll a molecules in five non-equivalent binding sites, with at least one chlorophyll a presenting a slight distortion to its macrocycle. The binding modes and conformations of HliD-bound pigments are discussed with respect to the known structures of LHCII and CP29.

Název v anglickém jazyce

Twisting a beta-Carotene, an Adaptive Trick from Nature for Dissipating Energy during Photoprotection

Popis výsledku anglicky

Cyanobacteria possess a family of one-helix high light-inducible proteins (Hlips) that are homologous to light-harvesting antenna of plants and algae. An Hlip protein, high light-inducible protein D (HliD) purified as a small complex with the Ycf39 protein is evaluated using resonance Raman spectroscopy. We show that the HliD binds two different beta-carotenes, each present in two non-equivalent binding pockets with different conformations, having their (0,0) absorption maxima at 489 and 522 nm, respectively. Both populations of beta-carotene molecules were in all-trans configuration and the absorption position of the farthest blue-shifted beta-carotene was attributed entirely to the polarizability of the environment in its binding pocket. In contrast, the absorption maximum of the red-shifted beta-carotene was attributed to two different factors: the polarizability of the environment in its binding pocket and, more importantly, to the conformation of its beta-rings. This second beta-carotene has highly twisted beta-rings adopting a flat conformation, which implies that the effective conjugation length N is extended up to 10.5 modifying the energetic levels. This increase in N will also result in a lower S-1 energy state, which may provide a permanent energy dissipation channel. Analysis of the carbonyl stretching region for chlorophyll a excitations indicates that the HliD binds six chlorophyll a molecules in five non-equivalent binding sites, with at least one chlorophyll a presenting a slight distortion to its macrocycle. The binding modes and conformations of HliD-bound pigments are discussed with respect to the known structures of LHCII and CP29.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

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

Návaznosti

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

Rok uplatnění

2017

Kód důvěrnosti údajů

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

Název periodika

Journal of Biological Chemistry

ISSN

0021-9258

e-ISSN

—

Svazek periodika

292

Číslo periodika v rámci svazku

4

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

8

Strana od-do

1396-1403

Kód UT WoS článku

000393339800021

EID výsledku v databázi Scopus

—