Blue copper proteins have been our central project but it is now almost finished. We have shown that these proteins do not strain the copper coordination sphere into an unnatural structure, as was generally believed before, and we have given alternative explanations to their unusual structure, spectra, reduction potentials, and low reorganisation energies. We will continue to study coupling elements for electron transfer, both for these proteins and the related cytochromes and iron-sulphur clusters. We will study model systems as well as experimentally characterised systems. We will also refine our methods to include the effect of the protein on the spectrum and reduction potentials.
Porphyrin proteins are another Important group of metal proteins.
We have shown that myoglobin probably discriminates between CO and 02 by a hydrogen bond rather than by steric strain. These calculations will be refined by inclusion of the protein. Moreover, we will study the reaction mechanisms of two proteins which insert ions into the porphyrin ring, ferrochelatase and magnesium chelatase. We have also studied cytochromes involved in electron transfer and plan to study cytochrome P450. One of our students works with the interpretation of crystal structures in a direct co-operation between with the molecular biophysics department here in Lund.