his.sePublications
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
Side-chain interactions in the plastocyanin-cytochrome f complex
University of Skövde, Department of Natural Sciences. Biochemistry and Biophysics, Department of Chemistry, Göteborg University, Sweden.ORCID iD: 0000-0002-3053-4543
Biochemistry and Biophysics, Department of Chemistry, Göteborg University, Sweden.
Deptartment of Molecular Biotechnology, Chalmers University of Technology, Göteborg, Sweden.
Leiden Institute of Chemistry, Leiden University, Gorlaeus Laboratories, Netherlands.
2000 (English)In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 39, no 17, 5022-5027 p.Article in journal (Refereed) Published
Abstract [en]

Cytochrome f and plastocyanin are redox partners in the photosynthetic electron-transfer chain. Electron transfer from cytochrome f to plastocyanin occurs in a specific short-lived complex. To obtain detailed information about the binding interface in this transient complex, the effects of binding on the backbone and side-chain protons of plastocyanin have been analyzed by mapping NMR chemical-shift changes. Cytochrome f was added to plastocyanin up to 0.3 M equiv, and the plastocyanin proton chemical shifts were measured. Out of approximately 500 proton resonances, 86% could be observed with this method. Nineteen percent demonstrate significant chemical-shift changes and these protons are located in the hydrophobic patch (including the copper ligands) and the acidic patches of plastocyanin, demonstrating that both areas are part of the interface in the complex. This is consistent with the recently determined structure of the complex [Ubbink, M., Ejdebäck, M., Karlsson, B. G., and Bendall, D. S. (1998) Structure 6, 323-335]. The largest chemical-shift changes are found around His87 in the hydrophobic patch, which indicates tight contacts and possibly water exclusion from this part of the protein interface. These results support the idea that electron transfer occurs via His87 to the copper in plastocyanin and suggest that the hydrophobic patch determines the specificity of the binding. The chemical-shift changes in the acidic patches are significant but small, suggesting that the acidic groups are involved in electrostatic interactions but remain solvent exposed. The existence of small differences between the present data and those used for the structure may imply that the redox state of the metals in both proteins slightly affects the structure of the complex. The chemical-shift mapping is performed on unlabeled proteins, making it an efficient way to analyze effects of mutations on the structure of the complex.

Place, publisher, year, edition, pages
American Chemical Society (ACS), 2000. Vol. 39, no 17, 5022-5027 p.
National Category
Biochemistry and Molecular Biology
Research subject
Natural sciences
Identifiers
URN: urn:nbn:se:his:diva-9897DOI: 10.1021/bi992757cISI: 000086737900007PubMedID: 10819966Scopus ID: 2-s2.0-0039591353OAI: oai:DiVA.org:his-9897DiVA: diva2:743778
Available from: 2014-09-05 Created: 2014-09-05 Last updated: 2016-02-08Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textPubMedScopus

Search in DiVA

By author/editor
Ejdebäck, Mikael
By organisation
Department of Natural Sciences
In the same journal
Biochemistry
Biochemistry and Molecular Biology

Search outside of DiVA

GoogleGoogle Scholar

Altmetric score

Total: 1255 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