The redox-active protein cytochrome c is a highly positively charged hemoglobin that
regulates cell fate decisions of life and death. Under normal physiological conditions …

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 …

Cyt c (cytochrome c) has been traditionally envisioned as rapidly diffusing in two dimensions
at the surface of the mitochondrial inner membrane when not engaged in redox reactions …

Regulation of mitochondrial activity allows cells to adapt to changing conditions and to
control oxidative stress, and its dysfunction can lead to hypoxia-dependent pathologies such …

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 …

Heme proteins are known to perform a plethora of biologically important functions. This
article reviews work that has been conducted on various class I cytochrome c proteins over a …

Over the last 50 years resonance Raman spectroscopy has become an invaluable tool for
the exploration of chromophores in biological macromolecules. Among them, heme proteins …

The alkaline-induced structural transitions of ferricytochrome c have been studied
intensively as a model for how changes in metal ligation contribute to protein function and …

Cytochrome has served as a model system for studying redox reactions, protein folding, and
more recently peroxidase activity induced by partial unfolding on membranes. This review …

The oxidized state of cytochrome c is a subject of continuous interest, owing to the multitude
of conformations which the protein can adopt in solution and on surfaces of artificial and cell …