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 …

Cytochrome c (cyt c) is a multifunctional protein with varying conformations. However, the
conformation of cyt c in its native environment, mitochondria, is still unclear. Here, we …

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 …

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 …

Thrombocytopenia 4 is an inherited autosomal dominant thrombocytopenia, which occurs
due to mutations in the human gene for cytochrome c that results in enhanced mitochondrial …

In the cell cytochrome, c performs different functions depending on the environment in which
it acts; therefore, it has been classified as a multifunction protein. When anchored to the …

Anaerobic ammonium-oxidizing (anammox) bacteria convert nitrite and ammonium via nitric
oxide (NO) and hydrazine into dinitrogen gas by using a diverse array of proteins, including …

Cytochrome c is known as an electron-carrying protein in the respiratory chain of
mitochondria. Over the last 20 years, however, alternative functions of this very versatile …

Comprehensive protein identification and concomitant structural probing of proteins are of
great biological significance. However, this is challenging to accomplish simultaneously in …