Inhibition of electric eel acetylcholinesterase by porphin compounds

Abstract Synthetic porphin compounds have been found to be reversible inhibitors of acetylcholinesterase from electric eel with K i values of μ M range. It seems that the number and position of fluorine on the phenyl ring and metal of an inhibitor play an important role for binding of an inhibitor to the enzyme active site. Synthetic porphin compounds have been found to be reversible inhibitors of acetylcholinesterase from electric eel with K i values of μM range. It seems that the number and position of fluorine on the phenyl ring and metal of an inhibitor play an important role for binding of an inhibitor to the enzyme active site.