Protection of Photosystem II from Photodamage during the Assembly of the Water Oxidizing Complex
(1999)- Abstract
- Photosystem II catalyses the light driven oxidation of water, which is a key reaction in oxygenic photosynthesis. This enzyme is, however, exposed to light induced degradation, which decreases the efficiency of the photosynthetic process. The work presented here deals with the situation when photosystem II is at a high risk of photodamage due to impaired electron donation from the water oxidising Mn cluster. In particular, events which occur during the light dependent formation of this cluster have been studied.
Assembly of the Mn cluster, i.e. photoactivation, was studied in a mutant strain of the green alga Chlamydomonas reinhardtii that lacks the 23 kDa extrinsic subunit of photosystem II. This mutant (FUD 39) shows... (More) - Photosystem II catalyses the light driven oxidation of water, which is a key reaction in oxygenic photosynthesis. This enzyme is, however, exposed to light induced degradation, which decreases the efficiency of the photosynthetic process. The work presented here deals with the situation when photosystem II is at a high risk of photodamage due to impaired electron donation from the water oxidising Mn cluster. In particular, events which occur during the light dependent formation of this cluster have been studied.
Assembly of the Mn cluster, i.e. photoactivation, was studied in a mutant strain of the green alga Chlamydomonas reinhardtii that lacks the 23 kDa extrinsic subunit of photosystem II. This mutant (FUD 39) shows an enhanced chloride dependence of water oxidation and an altered light dependence of the photoactivation process, compared to the wild type. It is proposed that Cl- is important for the correct assembly of the Mn cluster during photoactivation and that a low Cl- affinity results in a high susceptibility for photoinhibition during this process.
EPR and variable fluorescence measurements were performed in membrane preparations from dark grown and photoactivated FUD 39 cells. Photoactivation, in vivo, was found to result in changes in the electron transfer rates on the acceptor side of photosystem II and in the amount of the oxidised forms of cyt b559 and TyrD.
Mn deficient preparations, which lack water oxidising capacity, show a slow electron transfer rate between QA and QB on the acceptor side of photosystem II. This reaction becomes faster during the photoactivation process. A decreased rate of forward electron transport increases the probability for back reactions in photosystem II. This can be advantageous when photosystem II is at the risk of photodamage due to impaired water oxidising ability. Regulation of the electron transfer rate between QA and QB is suggested to be an important mechanism, in vivo, for protection of photosystem II against photodamage during photoactivation.
Oxidation of TyrD and cyt b559 was found to occur early in the photoactivation process, before the water oxidising complex was functional. This indicates that these compounds have physiological significance as auxiliary electron donors in photosystem II, when electron donation from the Mn cluster is inefficient. Moreover, cyt b559 becomes reduced when photoactivation is performed at a high light intensity that results in a high reductive pressure on the acceptor side of photosystem II. This indicates that cyt b559 is important for the release of both oxidative stress on the donor side and reductive stress on the acceptor side of photosystem II in vivo. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/39696
- author
- Rova, Maria LU
- supervisor
- opponent
-
- Dr Vass, Imre, Institute of Plant Physiology, Biological Research Center of the Hungarian Academy of Sciences, Szeged, Hungary
- organization
- publishing date
- 1999
- type
- Thesis
- publication status
- published
- subject
- keywords
- TyrosineD, cytochrome b559, Photoinhibition, Photoactivation, Botany, Botanik
- pages
- 100 pages
- publisher
- Maria Rova, Department of Chemistry, Karlstad University
- defense location
- Nils Alwalls rum, Sölvegatan 41, Lund
- defense date
- 1999-05-27 10:00:00
- external identifiers
-
- other:ISRN: LUNKDL/NKBK-99/1059-SE
- ISBN
- 91-628-3600-5
- language
- English
- LU publication?
- yes
- additional info
- Article: Rova M, Franzén L-G, Fredriksson P-O and Styring S. (1994) Photosystem II in a mutant of Chlamydomonas reinhardtii lacking the 23 kDa psbP protein shows increased sensitivity to photoinhibition in the absence of chloride. Photosynth. Res. 39, 75-83. Article: Rova M, Mc Ewen B, Fredriksson P-O, and Styring S. (1996) Photoactivation and photoinhibition are competing in a mutant of Chlamydomonas reinhardtii lacking the 23 kDa extrinsic subunit of photosystem II. J. Biol. Chem. 271, 28918-28924. Article: Rova M, Mamedov F, Magnuson A, Fredriksson P-O and Styring S. (1998) Coupled activation of the donor and the acceptor side of photosystem II during photoactivation of the oxygen evolving cluster. Biochemistry 37, 11039-11045. Article: Magnuson A, Rova M, Mamedov F, Fredriksson P-O and Styring S. (1999) The role of cytochrome b559 and tyrosineD in protection against photoinhibition during in vivo photoactivation of Photosystem II, Biochim. Biophys. Acta, 180-191. Article: Rova M, Mamedov F, Magnuson A, Fredriksson P-O and Styring S. Manuscript
- id
- dc168820-07eb-41a0-ba4a-003ebeb07a49 (old id 39696)
- date added to LUP
- 2016-04-04 11:51:26
- date last changed
- 2018-11-21 21:07:39
@phdthesis{dc168820-07eb-41a0-ba4a-003ebeb07a49,
abstract = {{Photosystem II catalyses the light driven oxidation of water, which is a key reaction in oxygenic photosynthesis. This enzyme is, however, exposed to light induced degradation, which decreases the efficiency of the photosynthetic process. The work presented here deals with the situation when photosystem II is at a high risk of photodamage due to impaired electron donation from the water oxidising Mn cluster. In particular, events which occur during the light dependent formation of this cluster have been studied.<br/><br>
<br/><br>
Assembly of the Mn cluster, i.e. photoactivation, was studied in a mutant strain of the green alga Chlamydomonas reinhardtii that lacks the 23 kDa extrinsic subunit of photosystem II. This mutant (FUD 39) shows an enhanced chloride dependence of water oxidation and an altered light dependence of the photoactivation process, compared to the wild type. It is proposed that Cl- is important for the correct assembly of the Mn cluster during photoactivation and that a low Cl- affinity results in a high susceptibility for photoinhibition during this process.<br/><br>
<br/><br>
EPR and variable fluorescence measurements were performed in membrane preparations from dark grown and photoactivated FUD 39 cells. Photoactivation, in vivo, was found to result in changes in the electron transfer rates on the acceptor side of photosystem II and in the amount of the oxidised forms of cyt b559 and TyrD.<br/><br>
<br/><br>
Mn deficient preparations, which lack water oxidising capacity, show a slow electron transfer rate between QA and QB on the acceptor side of photosystem II. This reaction becomes faster during the photoactivation process. A decreased rate of forward electron transport increases the probability for back reactions in photosystem II. This can be advantageous when photosystem II is at the risk of photodamage due to impaired water oxidising ability. Regulation of the electron transfer rate between QA and QB is suggested to be an important mechanism, in vivo, for protection of photosystem II against photodamage during photoactivation.<br/><br>
<br/><br>
Oxidation of TyrD and cyt b559 was found to occur early in the photoactivation process, before the water oxidising complex was functional. This indicates that these compounds have physiological significance as auxiliary electron donors in photosystem II, when electron donation from the Mn cluster is inefficient. Moreover, cyt b559 becomes reduced when photoactivation is performed at a high light intensity that results in a high reductive pressure on the acceptor side of photosystem II. This indicates that cyt b559 is important for the release of both oxidative stress on the donor side and reductive stress on the acceptor side of photosystem II in vivo.}},
author = {{Rova, Maria}},
isbn = {{91-628-3600-5}},
keywords = {{TyrosineD; cytochrome b559; Photoinhibition; Photoactivation; Botany; Botanik}},
language = {{eng}},
publisher = {{Maria Rova, Department of Chemistry, Karlstad University}},
school = {{Lund University}},
title = {{Protection of Photosystem II from Photodamage during the Assembly of the Water Oxidizing Complex}},
year = {{1999}},
}