Evidence for an unprecedented histidine hydroxyl modification on D2-His336 in Photosystem II of Thermosynechoccocus vulcanus and Thermosynechoccocus elongatus.

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.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Sugiura M,Koyama K,Umena Y,Kawakami K,Shen JR,Kamiya N,Boussac A

doi

10.1021/bi401213m

subject

Has Abstract

pub_date

2013-12-31 00:00:00

pages

9426-31

issue

52

eissn

0006-2960

issn

1520-4995

journal_volume

52

pub_type

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