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I am trying to visualize the spectrophotometric metabolite
intermediate complex formation by P450 inhibitors in purified human
I see a clear peak at 430nm. However the peak does not follow usual
kinetics. It appears more like a burst within 4-5 minutes followed by
a gradual decrease in the peak. My reasoning for such behaviour is
that the inhibitor just binds (weak interaction) to the heme followed
by gradual dissociation. There may not be any reactive metabolite
leading to heme or protein modification. However the peak is
conspicuous by its absence in reactions carried out without NADPH.
Any inputs regarding explaination for such unusual kinetics will be
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