Peroxynitrite is a short-lived and reactive biological oxidant formed from the diffusion-
controlled reaction of the free radicals superoxide (O2•–) and nitric oxide (• NO). In this …

Cytochrome c (Cytc) plays a vital role in the mitochondrial electron transport chain (ETC). In
addition, it is a key regulator of apoptosis. Cytc has multiple other functions including ROS …

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 …

Cytochrome c (cyt c) is a cationic hemoprotein of∼ 100 amino acid residues that exhibits
exceptional functional versatility. While its primary function is electron transfer in the …

Oxidative post-translational modification of proteins by molecular oxygen (O2)-and nitric
oxide (• NO)-derived reactive species is a usual process that occurs in mammalian tissues …

In addition to serving as respiratory electron shuttle, ferri-cytochrome c (cyt c) acts as a
peroxidase; ie, it catalyzes the oxidation of organic substrates by H2O2. This peroxidase …

Heme proteins are crucial for biological systems by performing diverse functions. Nature has
evolved diverse approaches to fine-tune the structure and function of heme proteins, of …

We report a resonance Raman and UV–vis characterization of the active site structure of
oxidatively modified forms of cytochrome c (Cyt-c) free in solution and in complexes with …

Cytochrome c (cyt c) can undergo reversible conformational changes under biologically
relevant conditions. Revealing these alternative cyt c conformers at the cell and tissue level …

Mitochondrial cytochrome c is a highly conserved protein in eukaryotes. Certain functions of
cytochrome c have been tuned during evolution. For instance, the intrinsic peroxidase …