Solution conformation of ferricytochrome c-551 from Pseudomonas stutzeri substrain ZoBell

The main chain protons and the majority of side chain protons have been ass igned for the ferric form of Pseudomonas stutzeri substrain ZoBell (America n Type Culture Collection 14405) cytochrome c-551. The chemical shifts were compared to those for the ferrous protein to determine the pseudocontact s hift contribution. These observed values were compared to contributions cal culated from the atomic coordinates of the ferrous cytochrome and an optimi zed effective room temperature g-tensor centered on the paramagnetic ferric iron. The agreement between observed and calculated values indicates that the conformations of the two forms are highly similar. (C) 1999 Academic Pr ess.