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 …

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

Cyclic voltammetry has shown that reduction-reoxidation processesof D. vulgaris
Hildenborough and D. desulfuricans Norway cytochromes c 3 correspond to rather fast …

Differential pulse polarography of cytochrome c 553 from Desulfovibrio vulgaris
Hildenborough shows the existence of a reduction peak at EP≈− 0.20 V (vs. Ag/AgCl …

Interfacial reactions of cytochrome c3 at a graphite electrode were studied in a neutral
medium by means of the differential pulse and cyclic voltammetry. It was found that …

Direct electron transfer between cytochrome c 3 from Desulfovibrio desulfuricans NCIMB
8372 and electrodes made of different materials was studied using cyclic voltammetry and …

The behavior of cytochrome c 3 from Desulfovibrio desulfuricans Norway has been
investigated at the basal-plane pyrolytic graphite electrode. The electrochemistry of this …

Potentiometric, pulse polarographic, and cyclic voltammetric techniques were used
toinvestigate the electrochemical behavior of cytochrome c3 of Desulfovibrio vulgaris, strain …

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

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 …