Pulsed NMR Study of the Structure of Cytochrome c

Abstract

The small size of cytochrome c and the natural presence in it of a fast-relaxing paramagnetic center, the low-spin heme iron, which becomes diamagnetic on reduction, make this protein attractive for NMR studies. Wüthrich (1970) has reviewed earlier research in this area. Here we analyze the results of our double NMR experiments (1970a, b; 1971) in terms of the models discussed by Takano et al. at this Symposium and draw conclusions about the electronic structure.