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It's a small heme protein found loosely associated with the inner membrane of the mitochondrion. It is a soluble protein, unlike other cytochromes, and is an essential component of the electron transfer chain. It is capable of undergoing oxidation and reduction, but does not bind oxygen. It transfers electrons between Complexes III and IV. Read all about it here: http://en.wikipedia.org/wiki/Cytochrome_c
The Cytochrome C amino acid sequence is different in
different species.
All species present in specific environments have similar Cytochrome C. Theoretically, this turns standard theories of evolution on their head as there is no blending of
Cytochrome C between Phyla, Families, Orders or Classes.
Cytochrome C is generally regarded as the universal catalyst of cellular respiration, forming a electron-bridge between the respirable substrates and oxygen within mitochondria.
The colour of Cytochrome C is due to a bound heme-Fe in an identical manner to haemoglobin. Consequently the electron-carrying protein of the mitochondrial transport path has a similar red-orange to bright orange-pink colour.
Changes in the amino-acid sequences of Cytochrome C are used by biochemical taxonomists to detect changes in species that have occurred during evolution.
The heme-bound form of Cytochrome C is technically Holocytochrome C.
Cytochrome C has a specific antibody called Anti-Holocytochrome C 2CYTC-199 which is specific to human, murine and rat Holocytochrome. The Holocytochrome of porcine, bovine and equine species are unreactive. As a result, the antibody is used in forensic science.
Cytochrome C is the only water soluble Cytochrome and is the most well-known of all the Cytochromes.
Without Cytochrome C, apoptosis could not occur as the protein is a vital intermediate in the pathway.
different species.
All species present in specific environments have similar Cytochrome C. Theoretically, this turns standard theories of evolution on their head as there is no blending of
Cytochrome C between Phyla, Families, Orders or Classes.
Cytochrome C is generally regarded as the universal catalyst of cellular respiration, forming a electron-bridge between the respirable substrates and oxygen within mitochondria.
The colour of Cytochrome C is due to a bound heme-Fe in an identical manner to haemoglobin. Consequently the electron-carrying protein of the mitochondrial transport path has a similar red-orange to bright orange-pink colour.
Changes in the amino-acid sequences of Cytochrome C are used by biochemical taxonomists to detect changes in species that have occurred during evolution.
The heme-bound form of Cytochrome C is technically Holocytochrome C.
Cytochrome C has a specific antibody called Anti-Holocytochrome C 2CYTC-199 which is specific to human, murine and rat Holocytochrome. The Holocytochrome of porcine, bovine and equine species are unreactive. As a result, the antibody is used in forensic science.
Cytochrome C is the only water soluble Cytochrome and is the most well-known of all the Cytochromes.
Without Cytochrome C, apoptosis could not occur as the protein is a vital intermediate in the pathway.
(continued)
Cytochrome C is capable of undergoing oxidation and reduction but fails to bind with oxygen.
Ion-exchange chromatography is the predominant method of purifying Cytochrome C.
Cytochrome C is one of the most stable proteins and long-term storage can be easily achieved by storing below �20 degrees C.
Cytochrome C is about 100 amino acids in length.
There are some species of Prokaryotes which do not contain Cytochrome C.
If you provide me with more information on your level of study of Cytochrome C, I'll provide you with further information - more complex if necessary!
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