Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Photosystem II: organization, function and regulation
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
2001 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

What makes plants, green algae and cyanobacteria so remarkable is their ability to convert light energy to chemical energy and at the same time evolve oxygen. In order to do so, they have developed a complex molecular machinery involving pigment and co-factor binding multi-protein complexes. Photosystem II is one of the protein complexes responsible for trapping photons and carrying out this energy conversion in a process where water is oxidized and molecular oxygen is released.

In this thesis, I have studied the organizational, functional and regulatory aspects of photosystem II. The results from these investigations can be summarized as follows: (i) A simple method was developed to isolate a highly pure, intact and active photosystem II complex containing the light-harvesting LHCII directly from thylakoid membranes. (ii) This so-called photosystem II supercomplex has properties similar to the membrane fragments enriched in photosystem II (BBY), but contain less of other non-photosystem II proteins, hence providing a better experimental alternative to these membrane fragments. (iii) A CP47 containing photosystem II reaction center with neither extrinsic proteins nor CP43 could be photoactivated to evolve oxygen, demonstrating that the latter proteins are not required for water oxidation. (iv) The re-association of the cyclophilin-like protein (TLP40) with the lumenal surface of the thylakoid membranes, which regulates dephosphorylation and turnover of the photosystem II reaction center protein, is dependent on both temperature and pH. (v) The association between TLP40 and the photosynthetic membranes may also involve the cytochrome b6/f complex.

Finally, a model is presented discussing the possibilities that a GTP-33-kDa complex could regulate the interaction between TLP40 and the thylakoid membranes in light. 

Place, publisher, year, edition, pages
Stockholm: Stockholm University , 2001. , 50 p.
National Category
Biological Sciences
Research subject
Biogeochemistry
Identifiers
URN: urn:nbn:se:su:diva-142294ISBN: 91-7265-268-3 (print)OAI: oai:DiVA.org:su-142294DiVA: diva2:1091980
Public defence
2001-06-07, 14:00 (English)
Opponent
Note

Härtill 5 uppsatser

Stockholms universitetsbiblioteks retrospektiva digitalisering. Avhandlingar 1906-2003.

Available from: 2017-04-28 Created: 2017-04-28 Last updated: 2017-07-10Bibliographically approved

Open Access in DiVA

No full text

Other links

PDF (Not accessible to users outside Sweden)
By organisation
Department of Biochemistry and Biophysics
Biological Sciences

Search outside of DiVA

GoogleGoogle Scholar

Total: 7 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf