Resonance Raman studies of pyrocatechase-inhibitor complexes.
The 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.
D001565:Benzoates; D050548:Catechol 1,2-Dioxygenase; D002396:Catechols / Q000037:antagonists & inhibitors; D002942:Circular Dichroism; D049308:Dioxygenases; D010105:Oxygenases / Q000037:antagonists & inhibitors; D010636:Phenols; D011485:Protein Binding; D011487:Protein Conformation; D011520:Protocatechuate-3,4-Dioxygenase; D011549:Pseudomonas / Q000201:enzymology; D013053:Spectrophotometry; D013059:Spectrum Analysis, Raman
D001565:Benzoates; D002396:Catechols; D010636:Phenols; D010105:Oxygenases; D049308:Dioxygenases; D050548:Catechol 1,2-Dioxygenase; D011520:Protocatechuate-3,4-Dioxygenase