Crystal structure and electron transfer properties of cytochrome c3.

Abstract

The crystal structure of cytochrome c3 from the sulfate-reducing bacteria Desulfovibrio desulfuricans, Norway strain, has been determined through the fitting of the recently completed primary structure to a 2.5 A resolution electron density map. The phase calculations were based on three mercurial derivatives; anomalous scattering data were used to refine the four heme iron positions. A preliminary refinement of the molecular model has led to a conventional crystallographic R factor of 34%. Cytochrome c3 is folded in two structural domains with one heme in each, the two other heme moieties lying in a large groove dividing the molecule. The core of the protein is the compact four-heme cluster which presents a relatively high degree of solvent exposure. The structural pattern of redox centers suggests that electron transfer might occur through direct contacts between some of the heme groups, via the overlapping system of pi oribitals or via intervening amino acid side chains or both.