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Biochim Biophys Acta. 2015 Feb;1847(2):276-285. doi: 10.1016/j.bbabio.2014.11.009. Epub 2014 Dec 3.

Assembly of oxygen-evolving Photosystem II efficiently occurs with the apo-Cytb559 but the holo-Cytb559 accelerates the recovery of a functional enzyme upon photoinhibition.

Author information

1
Proteo-Science Research Center, Ehime University, Bunkyo-cho, Matsuyama, Ehime 790-8577, Japan; Department of Chemistry, Graduate School of Science and Technology, Ehime University, Bunkyo-cho, Matsuyama, Ehime 790-8577, Japan; PRESTO, Japan Science and Technology Agency (JST), 4-1-8, Honcho, Kawauchi, Saitama 332-0012, Japan. Electronic address: miwa.sugiura@ehime-u.ac.jp.
2
Department of Chemistry, Graduate School of Science and Technology, Ehime University, Bunkyo-cho, Matsuyama, Ehime 790-8577, Japan.
3
Proteo-Science Research Center, Ehime University, Bunkyo-cho, Matsuyama, Ehime 790-8577, Japan.
4
iBiTec-S, CNRS UMR 8221, CEA Saclay, 91191 Gif-sur-Yvette, France. Electronic address: alain.boussac@cea.fr.

Abstract

Cytb559 in Photosystem II is a heterodimeric b-type cytochrome. The subunits, PsbE and PsbF, consist each in a membrane α-helix. Roles for Cytb559 remain elusive. In Thermosynechococcus elongatus, taking advantage of the robustness of the PSII variant with PsbA3 as the D1 subunit (WT*3), 4 mutants were designed hoping to get mutants nevertheless the obligatory phototrophy of this cyanobacterium. In two of them, an axial histidine ligand of the haem-iron was substituted for either a methionine, PsbE/H23M, which could be potentially a ligand or for an alanine, PsbE/H23A, which cannot. In the other mutants, PsbE/Y19F and PsbE/T26P, the environment around PsbE/H23 was expected to be modified. From EPR, MALDI-TOF and O2 evolution activity measurements, the following results were obtained: Whereas the PsbE/H23M and PsbE/H23A mutants assemble only an apo-Cytb559 the steady-state level of active PSII was comparable to that in WT*3. The lack of the haem or, in PsbE/T26P, conversion of the high-potential into a lower potential form, slowed-down the recovery rate of the O2 activity after high-light illumination but did not affect the photoinhibition rate. This resulted in the following order for the steady-state level of active PSII centers under high-light conditions: PsbE/H23M≈PsbE/H23A<< PsbE/Y19F≤PsbE/T26P≤WT*3. These data show i) that the haem has no structural role provided that PsbE and PsbF are present, ii) a lack of correlation between the rate of photoinhibition and the Em of the haem and iii) that the holo-Cytb559 favors the recovery of a functional enzyme upon photoinhibition.

KEYWORDS:

Cytb(559); Haem axial ligands; Photoinhibition; Photosystem II

PMID:
25481108
DOI:
10.1016/j.bbabio.2014.11.009
[Indexed for MEDLINE]
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