UV Excitation of Carotenoid Binding Proteins OCP and HCP: Excited-State Dynamics and Product Formation
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F22%3A43904805" target="_blank" >RIV/60076658:12310/22:43904805 - isvavai.cz</a>
Výsledek na webu
<a href="https://chemistry-europe.onlinelibrary.wiley.com/doi/epdf/10.1002/cptc.202100194" target="_blank" >https://chemistry-europe.onlinelibrary.wiley.com/doi/epdf/10.1002/cptc.202100194</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1002/cptc.202100194" target="_blank" >10.1002/cptc.202100194</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
UV Excitation of Carotenoid Binding Proteins OCP and HCP: Excited-State Dynamics and Product Formation
Popis výsledku v původním jazyce
Over the last decade the orange carotenoid protein (OCP) gained attention due to its role in photoprotection in cyanobacteria. Recently, other carotenoid binding proteins such as helical carotenoid proteins (HCPs) have been identified and characterized, although the function of the HCPs is not yet clarified. Here we have examined OCP1 and two HCPs, HCP2 and HCP3, from Tolypothrix PCC 7601 by ultrafast spectroscopy after excitation of both carotenoid canthaxanthin and amino acids tryptophan and tyrosine in UV at 275 nm. We find that the canthaxanthin S-1 lifetime remains the same 3.5 ps as for excitation of the carotenoid S-2 state, but the S* signal is significantly amplified by UV excitation. In contrast to the S-2 excitation, we observe a formation of the canthaxanthin radical cation at 900 nm for all three proteins after 275 nm excitation. In OCP1, UV light also enhances the amplitude of spectral band centered at 550 nm at longer delays. This band likely corresponds to the first photoproduct of the OCP photocycle, suggesting that excess energy excitation and/or direct excitation of amino acids can enhance the product formation.
Název v anglickém jazyce
UV Excitation of Carotenoid Binding Proteins OCP and HCP: Excited-State Dynamics and Product Formation
Popis výsledku anglicky
Over the last decade the orange carotenoid protein (OCP) gained attention due to its role in photoprotection in cyanobacteria. Recently, other carotenoid binding proteins such as helical carotenoid proteins (HCPs) have been identified and characterized, although the function of the HCPs is not yet clarified. Here we have examined OCP1 and two HCPs, HCP2 and HCP3, from Tolypothrix PCC 7601 by ultrafast spectroscopy after excitation of both carotenoid canthaxanthin and amino acids tryptophan and tyrosine in UV at 275 nm. We find that the canthaxanthin S-1 lifetime remains the same 3.5 ps as for excitation of the carotenoid S-2 state, but the S* signal is significantly amplified by UV excitation. In contrast to the S-2 excitation, we observe a formation of the canthaxanthin radical cation at 900 nm for all three proteins after 275 nm excitation. In OCP1, UV light also enhances the amplitude of spectral band centered at 550 nm at longer delays. This band likely corresponds to the first photoproduct of the OCP photocycle, suggesting that excess energy excitation and/or direct excitation of amino acids can enhance the product formation.
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
10610 - Biophysics
Návaznosti výsledku
Projekt
<a href="/cs/project/GX19-28323X" target="_blank" >GX19-28323X: Vztah mezi strukturou a funkcí karotenoidů: Nové cesty k řešení nezodpovězených otázek</a><br>
Návaznosti
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Ostatní
Rok uplatnění
2022
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
ChemPhotoChem
ISSN
2367-0932
e-ISSN
2367-0932
Svazek periodika
6
Číslo periodika v rámci svazku
1
Stát vydavatele periodika
DE - Spolková republika Německo
Počet stran výsledku
10
Strana od-do
nestrankovano
Kód UT WoS článku
000711724500001
EID výsledku v databázi Scopus
2-s2.0-85117924530