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pubmed-article:7397092pubmed:abstractTextThe resonance Raman spectra of native pyrocatechase 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 upsilon 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.lld:pubmed
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pubmed-article:7397092pubmed:articleTitleResonance Raman studies of pyrocatechase-inhibitor complexes.lld:pubmed
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