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

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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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ASJC Scopus subject areas

  • Biochemistry

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