Crystal structure of a dimeric octaheme cytochrome c3 (M(r) 26,000) from Desulfovibrio desulfuricans Norway.
Czjzek, M., Guerlesquin, F., Bruschi, M., Haser, R.(1996) Structure 4: 395-404
- PubMed: 8740362 
- DOI: https://doi.org/10.1016/s0969-2126(96)00045-7
- Primary Citation of Related Structures:  
1CZJ - PubMed Abstract: 
The octaheme cytochrome C3 (M(r) 26,000; cc3) from Desulfovibrio desulfuricans Norway is a dimeric cytochrome made up of two identical subunits, each containing four heme groups. It is involved in the redox transfer chain of sulfate-reducing bacteria, which links the periplasmic oxidation of hydrogen to the cytoplasmic reduction of sulfate. The amino-acid sequence of cc3 shows similarities to that of the tetraheme cytochrome c3 (M(r) 13,000; c3) from the same bacteria. Structural analysis of cc3 forms a basis for understanding the precise roles of the multiheme-containing redox proteins and the reason for the presence of several different multiheme cytochromes in one bacterial strain.
Organizational Affiliation: 
Laboratoire de Cristallographie et Cristallisation des Macromolécules Biologiques, URA 1296, CNRS, Marseille, France.