Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

Coupled Activation of the Donor and the Acceptor Side of Photosystem II during Photoactivation of the Oxygen Evolving Cluster

Rova, Maria ; Mamedov, Fikret LU ; Magnusson, Ann ; Fredriksson, Per-Olof and Styring, Stenbjörn LU (1998) In Biochemistry 37(31). p.11039-11045
Abstract
Photoactivation of photosystem II has been studied in the FUD 39 mutant of Chlamydomonas reinhardtii that lacks the 23 kDa extrinsic subunit of photosystem II. We have taken advantage of the slow photoactivation rate of FUD 39, earlier demonstrated in Rova, E. M., et al. [(1996) J. Biol. Chem. 271, 28918-28924], to study events in photosystem II during intermediate stages of the process. By measuring the EPR multiline signal, the decay of the variable fluorescence after single flashes, and electron transfer from water to the QB site, we found a good correlation between the building of a tetrameric Mn cluster, longer recombination times between QA- and the donor side of photosystem II, and the achievement of water splitting ability. An... (More)
Photoactivation of photosystem II has been studied in the FUD 39 mutant of Chlamydomonas reinhardtii that lacks the 23 kDa extrinsic subunit of photosystem II. We have taken advantage of the slow photoactivation rate of FUD 39, earlier demonstrated in Rova, E. M., et al. [(1996) J. Biol. Chem. 271, 28918-28924], to study events in photosystem II during intermediate stages of the process. By measuring the EPR multiline signal, the decay of the variable fluorescence after single flashes, and electron transfer from water to the QB site, we found a good correlation between the building of a tetrameric Mn cluster, longer recombination times between QA- and the donor side of photosystem II, and the achievement of water splitting ability. An increased rate of electron transfer from QA- to the QB site on the acceptor side of photosystem II, mainly due to enhanced efficiency of binding of QB to its site, was found to precede the building of the Mn cluster. We also showed that TyrD was oxidized simultaneously with this increase in electron-transfer rate. Thus, it appears that photoactivation is sequential, with an increased rate of electron transfer on the acceptor side occurring together with the oxidation of TyrD in the first step, followed by the assembly of the Mn cluster. We suggest that a conformational change of photosystem II is induced early in the photoactivation process facilitating electron transfer from the primary donor to the acceptor side. As a consequence, TyrD, an auxiliary electron donor to P680+/TyrZ, is oxidized. That this occurs before the Mn cluster is fully functional serves to protect photosystem II against donor side induced photodamage. (Less)
Please use this url to cite or link to this publication:
author
; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biochemistry
volume
37
issue
31
pages
11039 - 11045
publisher
The American Chemical Society (ACS)
external identifiers
  • scopus:0032483036
ISSN
0006-2960
language
English
LU publication?
yes
id
c0a14b5c-5914-4f27-9639-7b0fe1187365 (old id 125604)
alternative location
http://pubs.acs.org/cgi-bin/abstract.cgi/bichaw/1998/37/i31/abs/bi980381h.html
date added to LUP
2016-04-01 11:36:45
date last changed
2022-01-26 07:37:30
@article{c0a14b5c-5914-4f27-9639-7b0fe1187365,
  abstract     = {{Photoactivation of photosystem II has been studied in the FUD 39 mutant of Chlamydomonas reinhardtii that lacks the 23 kDa extrinsic subunit of photosystem II. We have taken advantage of the slow photoactivation rate of FUD 39, earlier demonstrated in Rova, E. M., et al. [(1996) J. Biol. Chem. 271, 28918-28924], to study events in photosystem II during intermediate stages of the process. By measuring the EPR multiline signal, the decay of the variable fluorescence after single flashes, and electron transfer from water to the QB site, we found a good correlation between the building of a tetrameric Mn cluster, longer recombination times between QA- and the donor side of photosystem II, and the achievement of water splitting ability. An increased rate of electron transfer from QA- to the QB site on the acceptor side of photosystem II, mainly due to enhanced efficiency of binding of QB to its site, was found to precede the building of the Mn cluster. We also showed that TyrD was oxidized simultaneously with this increase in electron-transfer rate. Thus, it appears that photoactivation is sequential, with an increased rate of electron transfer on the acceptor side occurring together with the oxidation of TyrD in the first step, followed by the assembly of the Mn cluster. We suggest that a conformational change of photosystem II is induced early in the photoactivation process facilitating electron transfer from the primary donor to the acceptor side. As a consequence, TyrD, an auxiliary electron donor to P680+/TyrZ, is oxidized. That this occurs before the Mn cluster is fully functional serves to protect photosystem II against donor side induced photodamage.}},
  author       = {{Rova, Maria and Mamedov, Fikret and Magnusson, Ann and Fredriksson, Per-Olof and Styring, Stenbjörn}},
  issn         = {{0006-2960}},
  language     = {{eng}},
  number       = {{31}},
  pages        = {{11039--11045}},
  publisher    = {{The American Chemical Society (ACS)}},
  series       = {{Biochemistry}},
  title        = {{Coupled Activation of the Donor and the Acceptor Side of Photosystem II during Photoactivation of the Oxygen Evolving Cluster}},
  url          = {{http://pubs.acs.org/cgi-bin/abstract.cgi/bichaw/1998/37/i31/abs/bi980381h.html}},
  volume       = {{37}},
  year         = {{1998}},
}