Hi everyone !!
I am working on a protein which binds to its ligand in a particular state
i.e. Fe3+ state (active) and reduces it to Fe2+ state (inactive). I am
trying to set up crystallisation trials with the ligand but seems like
difficult to get them. However i just needed an advice here, is
Hi Monica,
what is the reducing agent the protein gets the electron from?
Or is it simply unspecific oxidation of protein side chains?
Do you know what are the coordinating residues of Fe3+ / Fe2+ ?
Dependent on the coordination Fe3+ has some (often very weak) d-d
transitions (400-500 nm)
If it is a heme or ironsulfur cluster then the reduced and oxidized forms have
distinctly different spectra. Take a spectrum of your protein reduced with a
few grains of dithionite and oxidized with a trace of hydrogen peroxide or
ferricyanide (take another spectrum of ferricyanide alone since
