Structure of the Iron-Sulfur Cluster in the Chromatium Iron Protein at 2.25   Resolution

The high-potential iron-sulfur protein (HiPIP or HiPISP) of Chromatium vinosum, strain D, is representative of a widely occurring and highly diverse class of oxidation-reduction proteins, each of which contains one or more non-heme iron atoms and a variable complement of inorganic sulfide and cysteine. HiPIP consists of an 86 residue polypeptide chain (Dus et al., 1971) with four cysteines, and an inorganic prosthetic group composed of four sulfides and four iron atoms bound to the apoprotein by the cysteine sulfur atoms.