On the role of strain in blue copper proteins

Research output: Contribution to journalArticle


Theoretical investigations of the structure and function of the blue copper proteins are described. We have studied the optimum vacuum geometry of oxidised and reduced copper sites, the relative stability of trigonal and tetragonal Cu(II) structures, the relation between the structure and electronic spectra, the reorganisation energy, and reduction potentials. Our calculations give no support to the suggestion that strain plays a significant role in the function of these proteins; on the contrary, our results show that the structures encountered in the proteins are close to their optimal vacuum geometries (within 7 kJ/mol). We stress the importance of defining what is meant by strain and of quantifying strain energies or forces in order to make strain hypotheses testable.


  • Ulf Ryde
  • Mats H M Olsson
  • Björn O. Roos
  • Jan O A De Kerpel
  • Kristine Pierloot
External organisations
  • Catholic University of Leuven
Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Theoretical Chemistry


  • Blue copper proteins, Entatic state theory, Induced-rack theory, Protein strain, Quantum chemical calculations
Original languageEnglish
Pages (from-to)565-574
Number of pages10
JournalJournal of Biological Inorganic Chemistry
Issue number5
Publication statusPublished - 2000
Publication categoryResearch