Resonance Raman evidence for tyrosine involvement in the radical site of galactose oxidase

M. M. Whittaker, V. L. DeVito, S. A. Asher, J. W. Whittaker

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Abstract

Resonance Raman data are reported for the redox-activated form of galactose oxidase from Dactylium dendroides. Excitation within the red (659 nm) and blue (457.9 nm) absorption bands leads to strong resonance enhancement of ligated tyrosine vibrational modes at 550, 1170, 1247, 1484, and 1595 cm-1. The ring mode frequencies are unusually low, indicating a decreased bond order in the ring. The spectra clearly differ in both frequencies and relative intensities from those characteristic of known aromatic π-radicals. Enhancement of tyrosine ring modes on excitation within absorption bands previously associated with the presence of the radical in the active site suggests that the ligated tyrosine residue is present in the radical site and may stabilize this radical species through formation of a charge transfer complex. A dramatically different Raman spectrum is observed for the N3- adduct of galactose oxidase, exhibiting a single strong 1483 cm-1 feature. The intense visible-near IR absorption bands for galactose oxidase may derive from transitions within a charge transfer complex between an aromatic free radical and a tyrosine-copper complex.

Original languageEnglish (US)
Pages (from-to)7104-7106
Number of pages3
JournalJournal of Biological Chemistry
Volume264
Issue number13
StatePublished - Jan 1 1989

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ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Whittaker, M. M., DeVito, V. L., Asher, S. A., & Whittaker, J. W. (1989). Resonance Raman evidence for tyrosine involvement in the radical site of galactose oxidase. Journal of Biological Chemistry, 264(13), 7104-7106.