A thermodynamic model is presented to describe the redox behaviour of the tetraheme
cytochrome c3 from Desulfovibrio gigas. This molecule displays different intrinsic redox …

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 …

One of the aims of the intensive work undertaken to explore protein structure is to explain
variations in the properties of proteins at a structural level. In the case of haem-containing …

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 …

Three-quarters of the carbon-13 resonances of nuclei attached to the four haems of
Desulfovibrio uulgaris ferricytochrome c3 are assigned. Preliminary analysis of their Fermi …

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 …

The tetraheme cytochrome c554 (cyt c554) from Nitrosomonas europaea is an essential
electron transfer component in the biological oxidation of ammonia. The protein contains …

To specify electron exchanges involving Desulfovibrio desulfuricans Norway tetra‐heme
cytochrome c3, the chemical modification of arginine 73 residue performed. Biochemical …

The three-dimensional X-ray structure of cytochrome c 3 from sulfate-reducing bacteria
Desulfovibrio vulgaris Hildenborough (DvH)(M r 13 kDa, 107 residues, 4 heme groups) has …

A tetrahemic protein, cytochrome c 3 from Desulfovibrio desulfuricans strain Norway, is
studied by differential pulse polarography and linear sweep voltammetry at hanging mercury …