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

Result code in 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>

Alternative codes found

RIV/61388971:_____/17:00473562

Result on the web

<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>

Result language

angličtina

Original language name

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

Original language description

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.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10608 - Biochemistry and molecular biology

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

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

Publication year

2017

Confidentiality

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

Name of the periodical

Journal of Biological Chemistry

ISSN

0021-9258

e-ISSN

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Volume of the periodical

292

Issue of the periodical within the volume

4

Country of publishing house

US - UNITED STATES

Number of pages

8

Pages from-to

1396-1403

UT code for WoS article

000393339800021

EID of the result in the Scopus database

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