Covering: up to July 2008 A discussion of the literature concerning the synthesis, function,
and activity of hemec-containing proteins is presented. Comparison of the properties of …

A strength of NMR spectroscopy is its ability to monitor, on an atomic level, molecular
changes and interactions. In this review, which is intended for non‐spectroscopist, we …

Protein dynamics is intimately linked to function. In metalloproteins, dynamics are often
coupled to redox activity, ligand binding and enzyme function. We provide a concise …

Evolutionary conservation of substructure architecture between yeast iso‐1‐cytochrome c
and the well‐characterized horse cytochrome c is studied with limited proteolysis, the …

To study how proline residues affect the dynamics of Ω-loop D (residues 70 to 85) of
cytochrome c, we prepared G83P and G83A variants of yeast iso-1-cytochrome c (iso-1 …

Cytochrome c (cyt c) family proteins, such as horse cyt c, Pseudomonas aeruginosa
cytochrome c 551 (PA cyt c 551), and Hydrogenobacter thermophilus cytochrome c 552 (HT …

Direct electrochemical analysis of adsorbed bacterial monoheme cytochromes c has
revealed a phenomenological loss of the axial methionine when examined using pyrolytic …

The alkaline transition of cytochrome c involves substitution of the Met80 heme ligand of the
native state with a lysine ligand from a surface Ω-loop (residues 70 to 85). The standard …

The direct electrochemical analysis of adsorbed redox active proteins has proven to be a
powerful technique in biophysical chemistry, frequently making use of the electrode material …

Nonoverlapping closed loops of around 25–35 amino acids formed via nonlocal interactions
at the loop ends have been proposed as an important unit of protein structure. This …