Cytochromes are involved in a wide variety of redox reactions in living systems. Some of
them contain multiple hemes such as Desulfovibrio cytochrome c 3 and Shewanella small …

Tetrahaem cytochromes c 3 from sulfate-reducing bacteria have revealed exquisite
complexity in their ligand binding properties and they couple the cooperative binding of two …

Unique among sulphate-reducing bacteria, Desulfovibrio africanus has two periplasmic
tetraheme cytochromes c3, one with an acidic isoelectric point which exhibits an unusually …

The complete genome sequence of the δ-proteobacterium Geobacter sulfurreducens
reveals a large abundance of multiheme cytochromes. Cytochrome c 7, isolated from this …

The structure of dimeric cytochrome c3 from the sulfate-reducing bacterium Desulfovibrio
gigas, diDg, obtained by ab initio methods was further refined to 1.2 Å resolution, giving final …

The tetraheme cytochrome c 3 isolated from Desulfomicrobium baculatum (DSM
1743)(Dsmb) was cloned, and the sequence analysis showed that this cytochrome differs in …

Cytochromes c 7 are periplasmic triheme proteins that have been reported exclusively in δ-
proteobacteria. The structures of five triheme cytochromes identified in Geobacter …

Aromatic residues in c-type cytochromes might have an important function in the folding
and/or electron transferring properties of the molecule. In the tetraheme cytochrome c 3 (M r …

Cytochromes c 3 isolated from Desulfovibrio spp. are periplasmic proteins that play a central
role in energy transduction by coupling the transfer of electrons and protons from …

The roles of aromatic residues in redox regulation of cytochrome c 3 were investigated by
site-directed mutagenesis at every aromatic residue except for axial ligands (Phe20, Tyr43 …