Cytochrome C -Adis

Cytochrome CCytochrome C

Cytochrome C is a heme family protein 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 in order to form water. It transfers the electrons between the complex 3 and complex 4 of the respiratory chain or electron transport chain. 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 it has approximately 20% of its residues being Lysine (The Journal of Biochemistry). Cytochrome C, since it is so simple, 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 perfect beginner protein to experiment with. However simple, it is a very important 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 Structure Cytochrome C is a heme protein (or a part of the heme family) which means that it has a heme prosthetic group. This heme prosthetic group is covalently bonded using thioether bonds to cysteine residues. This heme prosthetic is eight cyclic structures forming a circle around a central iron atom. They can form different compounds by having different attachments around the 8 cyclic ring structure. Two conformations of cytochrome C exist naturally. In the monoheme form, the other axial position is usually left empty however, it can be occupied by other molecules such as histidine or lysine. Leaving the location empty prevents steric hindrance and allows for easier attachment. The other forms contain anywhere from one to seven methionine groups on what we perceive the left side of the heme group. When drawn out, the structure of Cytochrome C looks vertically and horizontally symmetrical due to the central heme group prior to adding side chains. The side chains which determine overall function are branched off of the central heme group and vary depending on the proteins location in the cell. They can have one form of side chain branching off at multiple locations, like a methionine attaching at multiple locations, or it can have different types of attachments, like one methionine at a location and then a lysine or histidine at another location. (Three-Dimensional Structure of Cytochrome c' ) Structural highlights This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.

spinqualitylabelsall models Caption for this structure Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image