Redox reactions play important roles in almost all biological processes, including
photosynthesis and respiration, which are two essential energy processes that sustain all life …

Redox potentials are a major contributor in controlling the electron transfer (ET) rates and
thus regulating the ET processes in the bioenergetics. To maximize the efficiency of the ET …

Abstract A water-soluble, 62-residue, di-α-helical peptide has been synthesized which
accommodates two bis-histidyl haem groups. The peptide assembles into a four-helix dimer …

Biological systems rely on heme-proteins to carry out a number of basic functions essential
for their survival. Hemes, or iron–porphyrin complexes, are the versatile and ubiquitous …

The free energy of heme reduction in different proteins is found to vary over more than 18
kcal/mol. It is a challenge to determine how proteins manage to achieve this enormous …

Iron-porphyrin complexes, known as hemes, form the prosthetic groups of a number of
proteins. These hemoproteins exhibit an impressive range of biological functions. These …

The thermodynamic properties of the Desulfovibrio vulgaris (Hildenborough) tetrahaem
cytochrome c3 (Dvc3) are rationalised by a model which involves both homotropic (e−/e−) …

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

The crystal structure of cytochrome c 3 (M r 13,000) from Desulfovibrio desulfuricans (118
residues, four heme groups) has been crystallographically refined to 1.7 Å resolution using a …

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 …