Resonance Raman Studies on Protocatechuate 3,4-Dioxygenase-Inhibitor Complexes

Lawrence Que, Robert M. Epstein

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Abstract

Resonance Raman spectra of a number of protocatechuate 3,4-dioxygenase-inhibitor complexes were studied by use of the available lines of an argon and a krypton laser. Three types of inhibitors were investigated-hydroxybenzoates, dicarboxylates, and 4-nitrocatechol. The hydroxybenzoate study shows that the hydroxy group in 3-hydroxybenzoate does not coordinate to the active site iron, in agreement with earlier suggestions, and confirms the coordination of the hydroxy group in the isomeric 4-hydroxybenzoate. The dicarboxylate study demonstrates that both glutarate and terephthalate perturb the active-site environment, shifting the charge-transfer interaction to lower energy. The pH dependence of tere-phthalate binding as well as the spectral similarities of the dicarboxylate complexes to the ESQ2 intermediate provides further evidence for the suggestion that this intermediate is a tightly bound enzyme-product complex. The 4-nitrocatechol study indicates that, unlike the substrate catechols, 4-nitrocatechol does not bind to the iron; a binding configuration wherein the acidic phenolate group interacts with the carboxylate binding site has been suggested by others. Finally the spectra of the 4-hydroxybenzoate and terephthalate complexes demonstrate the presence of two tyrosines coordinated to the active-site iron as suggested by others; these tyrosines have different vco's and excitation profiles.

Original languageEnglish (US)
Pages (from-to)2545-2549
Number of pages5
JournalBiochemistry
Volume20
Issue number9
DOIs
StatePublished - Apr 1981

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