The cupric geometry of blue copper proteins is not strained

Research output: Contribution to journalArticle


The geometry of several realistic models of the metal coordination sphere in the blue copper proteins has been optimised using high-level quantum chemical methods. The results show that the optimal vacuum structure of the Cu(II) models is virtually identical to the crystal structure of oxidised blue copper proteins. For the reduced forms, the optimised structure seems to be more tetrahedral than the one found in the proteins, but the energy difference between the two geometries is less than 5 kJ/mol, i.e. within the error limits of the method. Thus, the results raise strong doubts against hypotheses (entatic state and the induced-rack theory) suggesting that blue copper proteins force the oxidised metal coordination sphere into a structure similar to that preferred by Cu(I) in order to minimise the reorganisation energy of the electron transfer reaction. Instead, a small reorganisation energy seems to be reached by an appropriate choice of metal ligands. In particular, the cysteine thiolate ligand appears to be crucial, changing the preferred geometry of the oxidised complexes from square-planar to a more trigonal geometry.


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

Subject classification (UKÄ) – MANDATORY

  • Theoretical Chemistry


  • B3LYP method, Blue copper protein, Entatic state theory, Induced-rack theory, Protein strain
Original languageEnglish
Pages (from-to)586-596
Number of pages11
JournalJournal of Molecular Biology
Issue number4
Publication statusPublished - 1996 Aug 30
Publication categoryResearch