Department of Physical Chemistry, Faculty of Engineering, Yokohama National University,
Hodogaya-ku, Yokohama 240, Japan, and Institute for Protein Research, Osaka University …

Site-specific heme assignment of the 1 H-NMR spectrum of cytochrome c 3 of D. vulgaris
Miyazaki F, a tetraheme protein, was established. The major reduction of the heme turned …

The macroscopic standard (formal) potentials of the four hemes in cytochromes c 3 from
Desulfovibrio vulgaris Miyazaki (DvM) and Hildenborough (DvH), which Show reversible …

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 …

Using 2D-NMR the four haems of Desulfovibrio vulgaris (Hildenborough) cytochromes,
within the X-ray structure were fully cross-assigned according to their redox potential. The …

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 …

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 …

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

The assignment of 1H-NMR signals of the heme methyl and propionate groups of
cytochrome c3 of D. vulgaris Miyazaki F was performed. The heme assignment was revised …

Two kinds of high molecular mass cytochrome c 3 (Hmc) were isolated from Desulfovibrio
vulgaris Miyazaki, one from the membrane (mHmc), the other from the soluble fraction …