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The interaction of Cu (II) with the protein pepsin has been investigated by means of electron spin resonance (ESR) and optical spectroscopy. Depending on the molar ratio of Cu(II) and pepsin in aqueous solution two different complexes are formed. A third complex can be detected after a reaction time of several days, attributed to a complex with a conformationally changed pepsin. The presence of inhibitors 1,2-epoxy-3-phenoxypropane (EPP) or diazoacetyl-ethylester (DAE) seems to hinder the conformational change. The structure of the three complexes is discussed.

ESR and Optical Studies on the Interaction between Cu(II) and Pepsin