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 …

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 …

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 …

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

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 …

(1) Cytochromes c3 from Desulfovibrio vulgaris (Hildenborough strain) and Desulfovibrio
desulfuricans (Norway strain) have been studied by differential pulse polarography and …

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

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 …

The equilibrium oxidation-reduction mipoint potential (E m) of isolated Rhodopseudomonas
sphaeroides cytochrome c 2 exhibits a pH-dependent behavior which can be ascribed to ap …

Cytochrome c 553 is a monohaemic c type cytochrome isolated from the sulfate reducing
bacteria Desulfovibrio, vulgaris. Its midpoint potential value, determined by optical, EPR and …