Excited-State Properties of Canthaxanthin in Cyanobacterial Carotenoid-Binding Proteins HCP2 and HCP3

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F20%3A43901337" target="_blank" >RIV/60076658:12310/20:43901337 - isvavai.cz</a>

Výsledek na webu

<a href="https://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.0c03137" target="_blank" >https://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.0c03137</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1021/acs.jpcb.0c03137" target="_blank" >10.1021/acs.jpcb.0c03137</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Excited-State Properties of Canthaxanthin in Cyanobacterial Carotenoid-Binding Proteins HCP2 and HCP3

Popis výsledku v původním jazyce

Recently a new family of carotenoproteins, homologues of the N-terminal domain of the orange carotenoid protein (NTD-OCP), have been identified in cyanobacteria. These homologues are called helical carotenoid proteins (HCPs) as they are all predicted to maintain the all-helical structure of the NTD- OCP and to bind carotenoids. Here, HCP2 and HCP3 isolated from the cyanobacterium Tolypothrix PCC 7601 were studied by ultrafast transient absorption spectroscopy to explore the excited-state dynamics of the bound carotenoid, canthaxanthin. The lowest excited state, S-1 of canthaxanthin in both HCPs yields a lifetime of 3.5 ps; it is thus shorter than for canthaxanthin in solution (4.5 ps). This is because of the longer effective conjugation of canthaxanthin in HCPs, as one of the terminal rings is in an s-trans configuration. Use of two different excitation wavelengths, 470 and 570 nm, revealed excitation wavelength dependent spectroscopic response. Additional excited-state absorption bands are observed after excitation at 470 nm for both HCPs, proving the presence of more than one ground state conformer.

Název v anglickém jazyce

Excited-State Properties of Canthaxanthin in Cyanobacterial Carotenoid-Binding Proteins HCP2 and HCP3

Popis výsledku anglicky

Recently a new family of carotenoproteins, homologues of the N-terminal domain of the orange carotenoid protein (NTD-OCP), have been identified in cyanobacteria. These homologues are called helical carotenoid proteins (HCPs) as they are all predicted to maintain the all-helical structure of the NTD- OCP and to bind carotenoids. Here, HCP2 and HCP3 isolated from the cyanobacterium Tolypothrix PCC 7601 were studied by ultrafast transient absorption spectroscopy to explore the excited-state dynamics of the bound carotenoid, canthaxanthin. The lowest excited state, S-1 of canthaxanthin in both HCPs yields a lifetime of 3.5 ps; it is thus shorter than for canthaxanthin in solution (4.5 ps). This is because of the longer effective conjugation of canthaxanthin in HCPs, as one of the terminal rings is in an s-trans configuration. Use of two different excitation wavelengths, 470 and 570 nm, revealed excitation wavelength dependent spectroscopic response. Additional excited-state absorption bands are observed after excitation at 470 nm for both HCPs, proving the presence of more than one ground state conformer.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10610 - Biophysics

Projekt

<a href="/cs/project/GA18-21631S" target="_blank" >GA18-21631S: Ultrarychlá časová spektroskopie jako nástroj pro studium vztahu mezi strukturou a funkcí karotenoproteinů u sinic</a><br>

Návaznosti

S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2020

Kód důvěrnosti údajů

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

Název periodika

Journal of Physical Chemistry B

ISSN

1520-6106

e-ISSN

—

Svazek periodika

124

Číslo periodika v rámci svazku

24

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

10

Strana od-do

4896-4905

Kód UT WoS článku

000552403500004

EID výsledku v databázi Scopus

2-s2.0-85086749084