Direct spectroscopic evidence for a high-spin Fe(IV) intermediate in tyrosine hydroxylase

Bekir E. Eser, Eric W. Barr, Patrick A. Frantom, Lana Saleh, J. Martin Bollinger, Carsten Krebs, Paul F. Fitzpatrick

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Abstract

Tyrosine hydroxylase, a member of the aromatic amino acid hydroxylase family, uses a mononuclear Fe(II) and tetrahydropterin for hydroxylation of tyrosine to dihydroxyphenylalanine. Rapid-freeze quench Mössbauer spectroscopy has now provided direct evidence for the presence of an Fe(IV) intermediate in the reaction catalyzed by tyrosine hydroxylase. Rapid-quench techniques provide support for the kinetic competence of this species as the hydroxylating intermediate. This is the first direct evidence for a mononuclear Fe(IV) intermediate in an enzymatic aromatic hydroxylation reaction.

Original languageEnglish (US)
Pages (from-to)11334-11335
Number of pages2
JournalJournal of the American Chemical Society
Volume129
Issue number37
DOIs
StatePublished - Sep 19 2007

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ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

Cite this

Eser, B. E., Barr, E. W., Frantom, P. A., Saleh, L., Bollinger, J. M., Krebs, C., & Fitzpatrick, P. F. (2007). Direct spectroscopic evidence for a high-spin Fe(IV) intermediate in tyrosine hydroxylase. Journal of the American Chemical Society, 129(37), 11334-11335. https://doi.org/10.1021/ja074446s