We report the results of an EPR potentiometric titration of cytochrome c 3 from Desulfovibrio
vulgaris Miyazaki: the EPR spectral features of the four hemes are identified. The four …

The cytochrome c3 molecules are electron-transfer proteins isolated from the
sulphatereducing bacteria Desulfovibrio (Postgate & Campbell, 1966). They have mol. wts …

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 …

EPR spectroscopy in conjunction with oxidation-reduction potentiometry has been used to
determine the half-reduction potentials of the four hemes of cytochrome c 3. As predicted …

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 …

The EPR potentiometric titration for multihaemic cytochromes requires the measurement of
the intensity of the absorption EPR spectrum at different potential. We used this method to …

The electrochemical behaviour of cytochrome c 3 from Desulfovibrio desulfuricans, Norway
strain, remains unchanged within the pH range 5–9.5. Differential pulse polarography peaks …

Differential pulse and cyclic voltammetry studies with gold and glassy carbon electrodes of
tetrahemic cytochrome c 3 from Desulfovibrio desulfuricans Norway show the existence of …

An EPR redox titration was performed on the tetraheme cytochrome c3 isolated from
Desulfovibrio baculatus (strain 9974), a sulfate‐reducer. Using spectral differences at …

In cytochromes c3 which contain four hemes per molecule, the redox properties of each
heme may depend upon the redox state of the others. This effect can be described in terms …