InterPro domain: IPR003251

Rubrerythrin (Rr), found in anaerobic sulphate-reducing bacteria [ 1 ] and archaea, is a fusion protein containing an N-terminal diiron-binding domain and a C-terminal domain homologous to rubredoxin [ 2 ]. The physiological role of Rr has not been identified.

The 3-D structure of Desulphovibrio vulgaris rubrerythrin has been solved [ 3 ]. The structure reveals a tetramer of two-domainsubunits. In each monomer, the N-terminal 146 residues form a four-alpha-helix bundle containing the diiron-oxo site (centre I), and the C-terminal 45 residues form a rubredoxin-like FeS4 domain.

1. Characterization of three proteins containing multiple iron sites: rubrerythrin, desulfoferrodoxin, and a protein containing a six-iron cluster. Meth. Enzymol. 243, 216-40
2. The primary structure of rubrerythrin, a protein with inorganic pyrophosphatase activity from Desulfovibrio vulgaris. Comparison with hemerythrin and rubredoxin. J. Biol. Chem. 266, 20645-53
3. The structure of Desulfovibrio vulgaris rubrerythrin reveals a unique combination of rubredoxin-like FeS4 and ferritin-like diiron domains. Nat. Struct. Biol. 3, 539-46