Evidence for an unprecedented histidine hydroxyl modification on D2-His336 in photosystem II of thermosynechoccocus vulcanus and thermosynechoccocus elongatus

Miwa Sugiura, Kazumi Koyama, Yasufumi Umena, Keisuke Kawakami, Jian-Ren Shen, Nobuo Kamiya, Alain Boussac

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

The electron density map of the 3D crystal of Photosystem II from Thermosynechococcus vulcanus with a 1.9 Å resolution (PDB: 3ARC) exhibits, in the two monomers in the asymmetric unit cell, an, until now, unidentified and uninterpreted strong difference in electron density centered at a distance of around 1.5 Å from the nitrogen Nδ of the imidazole ring of D2-His336. By MALDI-TOF/MS upon tryptic digestion, it is shown that ∼20-30% of the fragments containing the D2-His336 residue of Photosystem II from both Thermosynechococcus vulcanus and Thermosynechococcus elongatus bear an extra mass of +16 Da. Such an extra mass likely corresponds to an unprecedented post-translational or chemical hydroxyl modification of histidine.

Original languageEnglish
Pages (from-to)9426-9431
Number of pages6
JournalBiochemistry
Volume52
Issue number52
DOIs
Publication statusPublished - Dec 31 2013

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Photosystem II Protein Complex
Histidine
Hydroxyl Radical
Carrier concentration
Electrons
Matrix-Assisted Laser Desorption-Ionization Mass Spectrometry
Chemical modification
Digestion
Nitrogen
Monomers
Crystals
imidazole

ASJC Scopus subject areas

  • Biochemistry

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Evidence for an unprecedented histidine hydroxyl modification on D2-His336 in photosystem II of thermosynechoccocus vulcanus and thermosynechoccocus elongatus. / Sugiura, Miwa; Koyama, Kazumi; Umena, Yasufumi; Kawakami, Keisuke; Shen, Jian-Ren; Kamiya, Nobuo; Boussac, Alain.

In: Biochemistry, Vol. 52, No. 52, 31.12.2013, p. 9426-9431.

Research output: Contribution to journalArticle

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abstract = "The electron density map of the 3D crystal of Photosystem II from Thermosynechococcus vulcanus with a 1.9 {\AA} resolution (PDB: 3ARC) exhibits, in the two monomers in the asymmetric unit cell, an, until now, unidentified and uninterpreted strong difference in electron density centered at a distance of around 1.5 {\AA} from the nitrogen Nδ of the imidazole ring of D2-His336. By MALDI-TOF/MS upon tryptic digestion, it is shown that ∼20-30{\%} of the fragments containing the D2-His336 residue of Photosystem II from both Thermosynechococcus vulcanus and Thermosynechococcus elongatus bear an extra mass of +16 Da. Such an extra mass likely corresponds to an unprecedented post-translational or chemical hydroxyl modification of histidine.",
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T1 - Evidence for an unprecedented histidine hydroxyl modification on D2-His336 in photosystem II of thermosynechoccocus vulcanus and thermosynechoccocus elongatus

AU - Sugiura, Miwa

AU - Koyama, Kazumi

AU - Umena, Yasufumi

AU - Kawakami, Keisuke

AU - Shen, Jian-Ren

AU - Kamiya, Nobuo

AU - Boussac, Alain

PY - 2013/12/31

Y1 - 2013/12/31

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AB - The electron density map of the 3D crystal of Photosystem II from Thermosynechococcus vulcanus with a 1.9 Å resolution (PDB: 3ARC) exhibits, in the two monomers in the asymmetric unit cell, an, until now, unidentified and uninterpreted strong difference in electron density centered at a distance of around 1.5 Å from the nitrogen Nδ of the imidazole ring of D2-His336. By MALDI-TOF/MS upon tryptic digestion, it is shown that ∼20-30% of the fragments containing the D2-His336 residue of Photosystem II from both Thermosynechococcus vulcanus and Thermosynechococcus elongatus bear an extra mass of +16 Da. Such an extra mass likely corresponds to an unprecedented post-translational or chemical hydroxyl modification of histidine.

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