We found that A. thaliana Sco1 binds both Cu(I) and Cu(II) with high affinity. We analyzed both copper sites by spectroscopic methods, XRay crystallograpy and DFT, confirming that Cu(I) tri-coordinated (2SCys-NeHis) and Cu(II) tetra-coordinated (2SCys-NeHis-H2O) (2/5)
To test the activity of AtSco1, we first designed a soluble model of AtCoxII. We confirmed the formation of CuA site and the possibility of monitoring all four possible oxidation and metallation states of the protein by NMR. (3/5)