Cytochromes c are haemoproteins which carry out electron transfer in a wide variety of
biological systems, necessitating different kinds of cytochrome c to fulfill different biological …

Iron-sulfur proteins constitute a group of electron transport proteins (ferredoxins) and
oxidation-reduction enzymes whose functionis now known to be central to such important …

The proton NMR spectra of the tetrahaem cytochrome c3 from Desulfovibrio gigas were
examined while varying the pH and the redox potential. The analysis of the NMR reoxidation …

Tetrahaem cytochromes c 3 from sulfate-reducing bacteria have revealed exquisite
complexity in their ligand binding properties and they couple the cooperative binding of two …

The redox potential of Ps. aeruginosa cytochrome c-551 varies with pH between pH 5 and 8.
The pH dependence can be analysed in terms of ap K a of 6.2 in the oxidised form and ap K …

High resolution nuclear magnetic resonance spectroscopy has been used to examine the
interaction of plastocyanins from French bean (Phaseolus vulgaris) and cucumber (Cucumis …

A purified preparation of hydrogenase from D. gigas was inactive toward ferredoxin,
flavodoxin or rubredoxin in the absence of cytochrome c 3 (MW 13,000), in an atmosphere of …

X-RAY crystallography and nuclear magnetic resonance (NMR) are the two most powerful
physical techniques for studying macromolecular structure. They are often used to …

Potentiometric titrations employing an electrochemical thin-layer cell indicate that complex
formation between ferredoxin and ferredoxin: NADP+ oxidoreductase alters the midpoint …

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 …