Using surface-modified electrodes composed of ω-hydroxyalkanethiols, an experimentally
based value for the inner-sphere reorganization energy of the bis (imidazole) iron porphyrin …

The spectral and electrochemical parameters, as well as the orientations of the heme planes
with respect to the membrane plane, of the c‐type hemes present in membrane fragments …

A thermodynamic model is presented to describe the redox behaviour of the tetraheme
cytochrome c3 from Desulfovibrio gigas. This molecule displays different intrinsic redox …

Cytochrome c-553 from Desulfovibrio vulgaris exhibits a highly exposed heme and an
unusually low reduction potential with respect to other c-type cytochromes. Solvent heme …

Reduction of the haems in tetrahaem cytochromes c 3 is a cooperative process, ie, reduction
of each of the haems depends on the redox states of the other haems. Furthermore, electron …

The pH‐induced protein conformational transitions and changes in the ligation state of the
heme iron in cytochrome c2 from Rhodopseudomonas palustris were monitored by …

Revised Manuscript Received June 19, 1995® abstract: The enthalpic and entropic
components of the redox free energy variation of cytochrome C553 from Desulfovibrio …

Trihaem cytochrome c3 (also known as cytochrome c551. 5 and cytochrome c7) is isolated
from the periplasmic space of Desulfuromonas acetoxidans, a sulfur‐reducing bacterium …

The reduction kinetics of two differently charged cytochromes c, horse cytochrome c and
Rhodosprillum rubrum cytochrome c 2, by ferrous EDTA 2− were studied as a function of …

NMR and visible spectroscopy were used to characterize the type II tetraheme cytochrome c
3 isolated from the periplasmic space of Desulfovibrio africanus, a sulfate-reducing …