title: On the role of strain in blue copper proteins.
abstract: 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.
authors.affiliation: Department of Theoretical Chemistry, Lund University, Chemical Centre, Sweden. ulf.ryde@teokem.lu.se
authors.forename: U
authors.initials: U
authors.lastname: Ryde
authors.forename: M H
authors.initials: MH
authors.lastname: Olsson
authors.forename: B O
authors.initials: BO
authors.lastname: Roos
authors.forename: J O
authors.initials: JO
authors.lastname: De Kerpel
authors.forename: K
authors.initials: K
authors.lastname: Pierloot
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism*; D003300:Copper / Q000378:metabolism; D004579:Electron Transport; D004583:Electrons; D008667:Metalloproteins / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D010084:Oxidation-Reduction; D011487:Protein Conformation; D011789:Quantum Theory; D013329:Structure-Activity Relationship
chemical_list: D001426:Bacterial Proteins; D008667:Metalloproteins; C017079:mauC protein, Methylobacterium extorquens; D003300:Copper