Hello
We studied the structure of the reduced and oxidized forms of cytochrome c
by spectroscopy at different wavelength (between 325 and 550 [nm])
particularly for the Soret band (gamma at 415 [nm]). The results seem to
show that the reduced form is much stable than the oxidized one when the pH
of the solution decrease or when urea (0 to 8 [mol*l-1]) was added to the
solution.
Does the additional electron of the Fe III form a new bond with an amino
acid of the peptide or does the more compact form of reduced cytochrome
include more inter-chain bonds ? What are the mechanism which make the
reduced form much stable than the oxidized ?
Thank's in advance !
Simon
