Carotenoid to bacteriochlorophyll energy transfer in the RC-LH1-PufX complex from Rhodobacter sphaeroides containing the extended conjugation keto-carotenoid diketospirilloxanthin

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F18%3A43897833" target="_blank" >RIV/60076658:12310/18:43897833 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60077344:_____/18:00495138

Výsledek na webu

<a href="https://link.springer.com/article/10.1007%2Fs11120-017-0397-4" target="_blank" >https://link.springer.com/article/10.1007%2Fs11120-017-0397-4</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s11120-017-0397-4" target="_blank" >10.1007/s11120-017-0397-4</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Carotenoid to bacteriochlorophyll energy transfer in the RC-LH1-PufX complex from Rhodobacter sphaeroides containing the extended conjugation keto-carotenoid diketospirilloxanthin

Popis výsledku v původním jazyce

RC-LH1-PufX complexes from a genetically modified strain of Rhodobacter sphaeroides that accumulates carotenoids with very long conjugation were studied by ultrafast transient absorption spectroscopy. The complexes predominantly bind the carotenoid diketospirilloxanthin, constituting about 75% of the total carotenoids, which has 13 conjugated C=C bonds, and the conjugation is further extended to two terminal keto groups. Excitation of diketospirilloxanthin in the RC-LH1-PufX complex demonstrates fully functional energy transfer from diketospirilloxanthin to BChl a in the LH1 antenna. As for other purple bacterial LH complexes having carotenoids with long conjugation, the main energy transfer route is via the S-2-Q(x) pathway. However, in contrast to LH2 complexes binding diketospirilloxanthin, in RC-LH1-PufX we observe an additional, minor energy transfer pathway associated with the S-1 state of diketospirilloxanthin. By comparing the spectral properties of the S-1 state of diketospirilloxanthin in solution, in LH2, and in RC-LH1-PufX, we propose that the carotenoid-binding site in RC-LH1-PufX activates the ICT state of diketospirilloxanthin, resulting in the opening of a minor S-1/ICT-mediated energy transfer channel.

Název v anglickém jazyce

Carotenoid to bacteriochlorophyll energy transfer in the RC-LH1-PufX complex from Rhodobacter sphaeroides containing the extended conjugation keto-carotenoid diketospirilloxanthin

Popis výsledku anglicky

RC-LH1-PufX complexes from a genetically modified strain of Rhodobacter sphaeroides that accumulates carotenoids with very long conjugation were studied by ultrafast transient absorption spectroscopy. The complexes predominantly bind the carotenoid diketospirilloxanthin, constituting about 75% of the total carotenoids, which has 13 conjugated C=C bonds, and the conjugation is further extended to two terminal keto groups. Excitation of diketospirilloxanthin in the RC-LH1-PufX complex demonstrates fully functional energy transfer from diketospirilloxanthin to BChl a in the LH1 antenna. As for other purple bacterial LH complexes having carotenoids with long conjugation, the main energy transfer route is via the S-2-Q(x) pathway. However, in contrast to LH2 complexes binding diketospirilloxanthin, in RC-LH1-PufX we observe an additional, minor energy transfer pathway associated with the S-1 state of diketospirilloxanthin. By comparing the spectral properties of the S-1 state of diketospirilloxanthin in solution, in LH2, and in RC-LH1-PufX, we propose that the carotenoid-binding site in RC-LH1-PufX activates the ICT state of diketospirilloxanthin, resulting in the opening of a minor S-1/ICT-mediated energy transfer channel.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10611 - Plant sciences, botany

Projekt

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

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2018

Kód důvěrnosti údajů

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

Název periodika

Photosynthesis Research

ISSN

0166-8595

e-ISSN

—

Svazek periodika

135

Číslo periodika v rámci svazku

1-3

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

11

Strana od-do

33-43

Kód UT WoS článku

000423338500005

EID výsledku v databázi Scopus

2-s2.0-85019548228