Determination of the geometric structure of the metal site in a blue copper protein by paramagnetic NMR.

ABSTRACT: The biological function of metalloproteins is closely tied to the geometric and electronic structures of the metal sites. Here, we show that the geometric structure of the metal site of a metalloprotein in solution can be determined from experimentally measured electron-nuclear spin-spin interactions obtained by NMR. Thus, the geometric metal site structure of plastocyanin from Anabaena variabilis was determined by including the paramagnetic relaxation enhancement of protons close to the copper site as restraints in a conventional NMR structure determination, together with the distribution of the unpaired electron onto the ligand atoms. Also, the interproton distances (nuclear Overhauser enhancements) and dihedral angles (scalar nuclear spin-spin couplings) normally used in NMR structure d

SUBMITTER: Hansen DF 

PROVIDER: S-EPMC1413626 | biostudies-literature | 2006 Feb

REPOSITORIES: biostudies-literature