Cytochrome C -Adis: Difference between revisions

==Cytochrome C==

Cytochrome C is a [http://en.wikipedia.org/wiki/All-α_proteins all-α proteins] family protein due to its alpha helical core that is generally located within the space between the inner mitochondrial membrane and outer mitochondrial membrane. It is a vital part of the respiratory cycle taking a key role in the transfer of electrons from complex III to complex IV. Cytochrome C is also one of the initiation proteins for apoptosis or cell death. One method of apoptosis is completely reliant on the release of cytochrome C into the cytosol in order to initiate apoptosis. Different conformations of Cytochrome C cause it to have different functions overall. The composition of Cytochrome C is relatively quite simple in comparison to other major proteins since approximately 20% of its residues being Lysine (The Journal of Biochemistry). Cytochrome C, since it is so small, is one of the most experimented on proteins out there. The structure being easy to map out and capable of being edited makes it a popular protein to experiment with even though it has the heme group causing some issues and complexity. However simple, it is a crucial protein for overall function in all Eukaryotes (New Journal of Science). It is also an ancient protein that established itself in the earliest stages of life but was not discovered until 1886 by Charles A. Macmunn. Cytochrome C was also rediscovered in 1925 by Charles Keilin. Since then, many have experimented with the inhibition of cytochrome C release which has shown promising results in therapeutic potential for Huntington’s disease. Others have used Cytochrome C in cancer research using it for its apoptosis function. The relatively small protein has a diverse job description causing it to be one of the most versatile experimental proteins known to this day.