Tocopherol controls D1 amino acid oxidation by oxygen radicals in Photosystem II.

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F21%3A73607818" target="_blank" >RIV/61989592:15310/21:73607818 - isvavai.cz</a>

Výsledek na webu

<a href="https://www.pnas.org/content/118/4/e2019246118" target="_blank" >https://www.pnas.org/content/118/4/e2019246118</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1073/pnas.2019246118" target="_blank" >10.1073/pnas.2019246118</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Tocopherol controls D1 amino acid oxidation by oxygen radicals in Photosystem II.

Popis výsledku v původním jazyce

Photosystem II (PSII) is an intrinsic membrane protein complex that functions as a light-driven water:plastoquinone oxidoreductase in oxygenic photosynthesis. Electron transport in PSII is associated with formation of reactive oxygen species (ROS) responsible for oxidative modifications of PSII proteins. In this study, oxidative modifications of the D1 and D2 proteins by the superoxide anion (O-2(center dot-)) and the hydroxyl (HO center dot) radicals were studied in WT and a tocopherol cyclase (vtel) mutant, which is deficient in the lipid-soluble antioxidant alpha-tocopherol. In the absence of this antioxidant, high-resolution tandem mass spectrometry was used to identify oxidation of D1:E-130 to hydroxyglutamic acid by O-2(center dot- ) at the Pheopi site. Additionally, D1:Y-246 was modified to either tyrosine hydroperoxide or dihydroxyphenylalanine by O(2)(center dot- )and HO center dot, respectively, in the vicinity of the nonheme iron. We propose that a-tocopherol is localized near Pheopi and the nonheme iron, with its chromanol head exposed to the lipid-water interface. This helps to prevent oxidative modification of the amino acid&apos;s hydrogen that is bonded to Pheopi and the nonheme iron (via bicarbonate), and thus protects electron transport in PSII from ROS damage.

Název v anglickém jazyce

Tocopherol controls D1 amino acid oxidation by oxygen radicals in Photosystem II.

Popis výsledku anglicky

Photosystem II (PSII) is an intrinsic membrane protein complex that functions as a light-driven water:plastoquinone oxidoreductase in oxygenic photosynthesis. Electron transport in PSII is associated with formation of reactive oxygen species (ROS) responsible for oxidative modifications of PSII proteins. In this study, oxidative modifications of the D1 and D2 proteins by the superoxide anion (O-2(center dot-)) and the hydroxyl (HO center dot) radicals were studied in WT and a tocopherol cyclase (vtel) mutant, which is deficient in the lipid-soluble antioxidant alpha-tocopherol. In the absence of this antioxidant, high-resolution tandem mass spectrometry was used to identify oxidation of D1:E-130 to hydroxyglutamic acid by O-2(center dot- ) at the Pheopi site. Additionally, D1:Y-246 was modified to either tyrosine hydroperoxide or dihydroxyphenylalanine by O(2)(center dot- )and HO center dot, respectively, in the vicinity of the nonheme iron. We propose that a-tocopherol is localized near Pheopi and the nonheme iron, with its chromanol head exposed to the lipid-water interface. This helps to prevent oxidative modification of the amino acid&apos;s hydrogen that is bonded to Pheopi and the nonheme iron (via bicarbonate), and thus protects electron transport in PSII from ROS damage.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10610 - Biophysics

Projekt

<a href="/cs/project/EF16_019%2F0000827" target="_blank" >EF16_019/0000827: Rostliny jako prostředek udržitelného globálního rozvoje</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>S - Specificky vyzkum na vysokych skolach

Rok uplatnění

2021

Kód důvěrnosti údajů

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

Název periodika

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

ISSN

0027-8424

e-ISSN

—

Svazek periodika

118

Číslo periodika v rámci svazku

4

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

10

Strana od-do

"2019246118-1"-"2019246118-10"

Kód UT WoS článku

000612945500056

EID výsledku v databázi Scopus

2-s2.0-85100011586