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

The first three-dimensional structure of a dimeric, octa-heme cytochrome c 3 (M r 26000)
from Desulfovibrio desulfuricans Norway, established at 2.2 Å resolution, is briefly presented …

Cytochrome c3 (M (r) 13,000) is a tetrahemic cytochrome in which the four heme iron atoms
are coordinated by 2 histidine residues at the axial positions. The presence of several …

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 …

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 …

Revised Manuscript Received April 13, 1993 abstract: The conformational change coupled
to the redox processes of two tetraheme cytochromes c3 from bacteria of the genus …

Desulfovibrio desulfuricans Norway cytochrome c 3 has been studied in various states of
oxidation by proton nuclear magnetic resonance at 360 and 500 MHz. NMR spectra …

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 6A is a unique dithio-cytochrome of green algae and plants. It has a very
similar core structure to that of bacterial and algal cytochromes c 6, but is unable to fulfil the …