The structure of a novel c7‐type cytochrome domain that has two bishistidine coordinated
hemes and one heme with histidine, methionine coordination (where the sixth ligand is a …

The structure of a cytochrome c 7 (PpcA) from Geobacter sulfurreducens was determined by
X-ray diffraction at 1.45 Å resolution; the R factor is 18.2%. The protein contains a three …

Multiheme cytochromes c are important in electron transfer pathways in reduction of both
soluble and insoluble Fe (III) by Geobacter sulfurreducens. We determined the crystal …

Crystals of the tetraheme cytochrome c3 from sulfate‐reducing bacteria Desulfovibrio gigas
(Dg)(MW 13 kDa, 111 residues, four heme groups) were obtained and X‐ray diffraction data …

Tetraheme cytochrome c 3 (cyt c 3) exhibits extremely low reduction potentials and unique
properties. Since axial ligands should be the most important factors for this protein, every …

The nature of the axial ligands of a heme group is an important factor in maintaining the
oxidation-reduction potential of a c-type cytochrome. Cytochrome c3 from Desulfovibrio …

Cytochrome c 7, a low potential, three heme-containing protein (molecular weight 9800) was
isolated from Desulfuromonas acetoxidans and crystallized from polyethylene glycol …

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

Cytochrome c 3 (M r 26000) isolated from Desulfovibrio gigas is a dimeric cytochrome
consisting of two identical subunits of 109 amino acids, each of which contains four haem …

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 …