Absorption and circular dichroism spectra of different forms of mushroom tyrosinase.
The circular dichroism spectrum of resting mushroom tyrosinase between 800 and 400 nm showed two bands at 755, and 653 nm. The CD spectrum of resting tyrosinase between 400 and 250 nm showed oxygen-sensitive changes at 350 nm upon treatment of tyrosinase with hydroxylamine or hydrogen peroxide. These were similar to changes observed on regeneration of aged hemocyanin by similar procedures. A structural relationship between the active sites of hydroxylamine- or hydrogen peroxide-treated tyrosinase and hemocyanin is suggested by these observations, confirming inferences based upon other studies (Jolly, Jr., R.L., Evans, L.H., Makino, N. and Mason, H.S. (1974) J. Biol. Chem. 249, 335-345 and Schoot Uiterkamp, A.J.M. and Mason, H.S. (1973) Proc. Natl. Acad, Sci. U.S. 70, 993-996).
D000363:Agaricales / Q000201:enzymology*; D001665:Binding Sites; D004156:Catechol Oxidase / Q000378:metabolism; D002942:Circular Dichroism; D004578:Electron Spin Resonance Spectroscopy; D006898:Hydroxylamines / Q000494:pharmacology; D007527:Isoenzymes / Q000378:metabolism; D014442:Monophenol Monooxygenase / Q000378:metabolism; D010100:Oxygen; D011485:Protein Binding; D011487:Protein Conformation; D013053:Spectrophotometry
D006898:Hydroxylamines; D007527:Isoenzymes; D004156:Catechol Oxidase; D014442:Monophenol Monooxygenase; D010100:Oxygen