Many molecules which contain several electroactive sites undergo successive electron
transfer reactions. It has been shown that cytochrome c3 from various sulfate reducing …

Cytochrome c3 is an electron transport protein with four c-type hemes found in sulfate-
reducing bacteria. The crystal structure of this protein has been establishedfor Desulfovibrio …

Abstract Cytochrome c-551.5 of the anaerobic sulfur-reducing bacterium Desulfuromonas
acetoxidans has been purified to homogeneity and characterized. It elicits absorption bands …

A new c-type cytochrome containing a single heme group, cytochrome c 553 (550) has been
purified from Desulfovibrio desulfuricans (Norway strain) and some of its properties have …

REDOX STATES OF CYTOCHROME c3 IN THE ABSENCE AND PRESENCE OF
FERREDOXIN 1. Introduction 2. Materials and methods Page 1 Volume 81, number 2 FEBS …

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 …

Cytochrome c 7, a low potential, three heme-containing protein (molecular weight 9800) was
isolated from Desulfuromonas acetoxidans and crystallized from polyethylene glycol …

The electron transfer reaction of Desulfovibrio vulgaris Hildenborough cytochrome c 3 at the
mercury and the pyrolytic graphite electrode was investigated using differential pulse and …

The reduction of cytochrome c 3 from Desulfovibrio vulgaris by dithionite or carboxyl radicals
follows biphasic kinetics. The data are consistent with lack of heme to heme electron …