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 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 …

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 …

Electron transfer in tetrahemic cytochromes c 3 from Desulfovibrio vulgaris Hildenborough
(DvH) and Desulfovibrio desulfuricans Norway (DdN) strains has been investigated by thin …

Reduction of the haems in tetrahaem cytochromes c 3 is a cooperative process, ie, reduction
of each of the haems depends on the redox states of the other haems. Furthermore, electron …

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 3 possesses four hemes in a compact configuration and exhibits extremely
low reduction potentials. Besides the well-characterized factors contributing to the reduction …

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 …

A combination of structural, kinetic, and interaction experiments has been used to study the
role of a highly conserved aromatic residue, Tyr73, parallel to the sixth heme axial ligand of …

Heteronuclear NMR spectroscopy was performed to determine the solution structure of 15N-
labeled ferrocytochrome c3 from Desulfovibrio vulgaris Miyazaki F (DvMF). Although the …