Resonance Raman Studies of Pyrocatechase-Inhibitor Complexes

The resonance Raman spectra of native pyro-catechase and its benzoate and phenolate complexes were investigated by using the available lines of an argon and a krypton laser. The data provide evidence for the presence of two distinct tyrosines coordinated to the active-site iron. The two tyrosines exhibit different v_co values which show maximum resonance enhancements at different excitation wavelengths. Moreover, one tyrosine is more susceptible to changes in the active-site environment. Pyrocatechase is the only example thus far among iron-tyrosinate proteins where the tyrosines coordinating the iron are distinguishable.