Amino acid oxidation of the D1 and D2 proteins by oxygen radicals during photoinhibition of Photosystem II
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F17%3A73584058" target="_blank" >RIV/61989592:15310/17:73584058 - isvavai.cz</a>
Result on the web
<a href="http://www.pnas.org/content/114/11/2988.full" target="_blank" >http://www.pnas.org/content/114/11/2988.full</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1073/pnas.1618922114" target="_blank" >10.1073/pnas.1618922114</a>
Alternative languages
Result language
angličtina
Original language name
Amino acid oxidation of the D1 and D2 proteins by oxygen radicals during photoinhibition of Photosystem II
Original language description
The Photosystem II reaction center is vulnerable to photoinhibition. The D1 and D2 proteins, lying at the core of the photosystem, are susceptible to oxidative modification by reactive oxygen species that are formed by the photosystem during illumination. Using spin probes and EPR spectroscopy, we have determined that both O2•− and HO• are involved in the photoinhibitory process. Using tandem mass spectroscopy, we have identified a number of oxidatively modified D1 and D2 residues. Our analysis indicates that these oxidative modifications are associated with formation of HO• at both the Mn4O5Ca cluster and the nonheme iron. Additionally, O2 •− appears to be formed by the reduction of O2 at either PheoD1 or QA. Early oxidation of D1:332H,which is coordinatedwith theMn1 of the Mn4O5Ca cluster, appears to initiate a cascade of oxidative events that lead to the oxidative modification of numerous residues in the C termini of the D1 and D2 proteins on the donor side of the photosystem. Oxidation of D2:244Y, which is a bicarbonate ligand for the nonheme iron, induces the propagation of oxidative reactions in residues of the D-de loop of the D2 protein on the electron acceptor side of the photosystem. Finally, D1:130E and D2:246Mare oxidatively modified by O2 •− formed by the reduction of O2 either by PheoD•− or QA•−. The identification of specific amino acid residues oxidized by reactive oxygen species provides insights into the mechanism of damage to the D1 and D2 proteins under light stress.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10610 - Biophysics
Result continuities
Project
<a href="/en/project/LO1204" target="_blank" >LO1204: Sustainable development of research in the Centre of the Region Haná</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2017
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Proceedings of the National Academy of Sciences of the USA
ISSN
0027-8424
e-ISSN
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Volume of the periodical
114
Issue of the periodical within the volume
11
Country of publishing house
US - UNITED STATES
Number of pages
6
Pages from-to
"2988–2993"
UT code for WoS article
000396094200060
EID of the result in the Scopus database
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