Cytochrome c (cyt c) is a small soluble heme protein characterized by a relatively flexible
structure, particularly in the ferric form, such that it is able to sample a broad conformational …

A novel cyclic dipeptide—cyclo [(S)-His-(S)-NorArg]—has been prepared which catalyzes an
enantioselective version of the Strecker amino acid synthesis. The catalyst, when present in …

The 1.94 A˚ resolution three-dimensional structure of oxidized horse heart cytochrome c has
been elucidated and refined to a final R-factor of 0.17. This has allowed for a detailed …

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 …

Organic chemists working on the synthesis of natural products have long found a special
challenge in the preparation of peptides and proteins. However, more reliable, more efficient …

High-resolution three-dimensional structural analyses of yeast iso-1-cytochrome c have now
been completed in both oxidation states using isomorphous crystalline material and similar …

Abstract Cytochrome-c (cyt-c), a multi-functional protein, plays a significant role in the
electron transport chain, and thus is indispensable in the energy-production process …

The pH-dependent conformational equilibria of iso-1-ferricytochrome c that occur between
pH 7 and pH 12 have been studied by resonance Raman (RR) spectroscopy. Detailed …

The nature of the axial ligation to heme iron has been suggested to be the major
determinant of the oxidation-reduction potential of a particular cytochrome, but natural …

It has been suggested that the alkaline form of cytochrome c (cyt c) regulates function of this
protein as an electron carrier in oxidative phosphorylation and as a peroxidase that reacts …