CYTOCHROME C & CLADISTICS

Cytochrome c is a small heme protein, consisting of about 100

amino acids, found loosely associated with the inner membranes
of mitochondria in all eukaryotic species. It is an essential
component of the electron transport chain (ETC), where it
transfers one electron between Complex III (cytochrome
b) and Complex IV (cytochrome oxidase) carriers. It is
capable of undergoing oxidation and reduction but does
not bind oxygen. The Cytochrome c protein is encoded by
the CYCS gene (on chromosome 7 in humans).

Cytochrome c is a highly conserved protein across the spectrum of species, found

in plants, animals and many unicellular organisms. This, along with its small size makes
it useful in the study of cladistics and evolutionary biology. (Cladistics is a method of
classification of organisms according to the proportion of measurable characteristics that
they have in common. It is assumed that the higher the proportion of characteristics that two
organisms share, the more recently they diverged from a common ancestor.) The primary
structure of cytochrome c consists of about 100 amino acids. The sequence of amino acids in
cytochrome c in humans is identical to
that in chimpanzees (our closest
relative) but differs in other species,
more distant in the evolutionary tree.
Differences in amino acid sequences
result from mutations of the CYCS
gene. In general, there is a predictable
rate of mutations over time so the
argument goes that the greater the total
of mutations and thus differences in
the amino acid sequences, the greater
is the evolutionary distance between
species. The chart compares amino
acid differences in cyctochrome c in
humans with some other species.

Comparing the sequences of the amino acids of cytochrome c has been fundamental to adding
support to Carl Woese's 1990 proposal which classifies all species into three domains,
replacing the previous system of 5 or 6 Kingdoms. Woese used ribsomal RNA (rRNA) as his
molecular marker and palced all living things into Domains: ARCHAEA, BACTERIA or
EUKARYOTA. And within those three domains, further groupings are confirmed by comparing
the amino acid sequences of cytochrome c, as well as other molecules.
Similar
comparisons of amino acid sequences have been made using haemoglobin, the oxygen carrying
molecule on red blood cells of the vertebrates. The table below indicates relationships.