4-Hydroxyphenylpyruvate dioxygenase is an iron-tyrosinate protein.
A resonance Raman investigation into the blue chromophore of 4-hydroxyphenylpyruvate dioxygenase, a non-heme iron enzyme from Pseudomonas P. J. 874, reveals the presence of enhanced vibrations characteristic of tyrosinate coordination to the iron center. The excitation profiles for these features show that they are associated with the 595 nm absorption feature. EPR studies of this enzyme indicate the presence of a high-spin ferric center in a rhombic environment, as evidenced by a signal at g = 4.3 with the correct intensity for the measured iron content. This enzyme thus belongs to the emerging class of iron-tyrosinate proteins.
D015111:4-Hydroxyphenylpyruvate Dioxygenase / Q000378:metabolism*; D004578:Electron Spin Resonance Spectroscopy / Q000379:methods; D007501:Iron / Q000032:analysis*; D010105:Oxygenases / Q000378:metabolism*; D011549:Pseudomonas / Q000201:enzymology; D013059:Spectrum Analysis, Raman / Q000379:methods; D014443:Tyrosine / Q000032:analysis*
D014443:Tyrosine; D007501:Iron; D010105:Oxygenases; D015111:4-Hydroxyphenylpyruvate Dioxygenase