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 …

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 …

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 refined structures of the cytochrome c 3 molecules from Desulfovibrio vulgaris Miyazaki
and Hildenborough have been compared in detail. Though there are no significant …

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 …

The structural basis for the pH dependence of the redox potential in the tetrahemic
Desulfovibrio vulgaris (Hildenborough) cytochrome c 3 was investigated by site-directed …

Cytochrome c-553 from Desulfovibrio vulgaris exhibits a highly exposed heme and an
unusually low reduction potential with respect to other c-type cytochromes. Solvent heme …

The cytochrome c553 from Desulfovibrio vulgaris (DvH c553) is of importance in the
understanding of the relationship of structure and function of cytochrome c due to its lack of …

We present a new examination of the EPR redox titration data for the tetraheme cytochrome
c3 from Desulfovibrio vulgaris Miyazaki. Our analysis includes the contribution of the …

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