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
Theoretical Investigations of Structure and Mechanism of the Oxygen-evolving Complex in PSII
Stockholm University, Faculty of Science, Department of Physics.
2004 In: Physical Chemistry Chemical Physics, ISSN 1463-9084, Vol. 6, no 20, 4772-4780 p.Article in journal (Refereed) Published
Place, publisher, year, edition, pages
2004. Vol. 6, no 20, 4772-4780 p.
Identifiers
URN: urn:nbn:se:su:diva-23780OAI: oai:DiVA.org:su-23780DiVA: diva2:194507
Note
Part of urn:nbn:se:su:diva-486Available from: 2005-04-27 Created: 2005-04-27Bibliographically approved
In thesis
1. Challenges in Enzyme Catalysis - Photosystem II and Orotidine Decarboxylase: A Density Functional Theory Treatment
Open this publication in new window or tab >>Challenges in Enzyme Catalysis - Photosystem II and Orotidine Decarboxylase: A Density Functional Theory Treatment
2005 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

Possibly the most fascinating biochemical mechanism remaining to be solved is the formation of oxygen from water in photosystem II. This is a critical part of the photosynthetic reaction that makes solar energy accessible to living organisms.

The present thesis uses quantum chemistry, more specifically the density functional B3LYP, to investigate a mechanism where an oxyl radical bound to manganese is the active species in O-O bond formation. Benchmark calculations on manganese systems confirm that B3LYP can be expected to give accurate results. The effect of the self-interaction error is shown to be limited. Studies of synthetic manganese complexes support the idea of a radical mechanism. A manganese complex with an oxyl radical is active in oxygen formation while manganese-oxo complexes remain inactive. Formation of the O-O bond requires a spin transition but there should be no effect on the rate. Spin transitions are also required in many short-range electron-transfer reactions.

Investigations of the superproficient enzyme orotidine decarboxylase support a mechanism that involves an invariant network of charged amino acids, acting together with at least two mobile water molecules.

Place, publisher, year, edition, pages
Stockholm: Fysikum, 2005. 77 p.
Keyword
photosystem II, oxyl radical, manganese systems, orotidine decarboxylase, reaction mechanism, density functional theory
National Category
Theoretical Chemistry
Identifiers
urn:nbn:se:su:diva-486 (URN)91-7155-057-7 (ISBN)
Public defence
2005-05-27, sal FA32, AlbaNova universitetscentrum, Roslagstullsbacken 21, Stockholm, 10:00
Opponent
Supervisors
Available from: 2005-04-27 Created: 2005-04-27Bibliographically approved

Open Access in DiVA

No full text

By organisation
Department of Physics

Search outside of DiVA

GoogleGoogle Scholar

urn-nbn

Altmetric score

urn-nbn
Total: 30 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