Copper-promoted overall transformation of 4-tert-butylphenol to its para-hydroxyquinonic derivative, 2-hydroxy-5-tert-butyl-1,4-benzoquinone. Biomimetic studies on the generation of topaquinone in copper amine oxidases

Bioorg Med Chem Lett. 2000 May 1;10(9):989-92. doi: 10.1016/s0960-894x(00)00145-1.

Abstract

Topaquinone (TPQ) is a cofactor present at the active site of copper amine oxidases, derived from a Tyr residue inserted in the polypeptide chain through a copper-dependent but otherwise largely unknown mechanism. A simple model system was developed that permits to obtain the overall transformation of 4-tert-butylphenol, chosen as a model for Tyr, into a TPQ-like, para-hydroxyquinonic structure in the presence of Cu(II)-imidazole mononuclear complexes.

MeSH terms

  • Amine Oxidase (Copper-Containing) / metabolism*
  • Benzoquinones / chemical synthesis*
  • Copper / chemistry*
  • Dihydroxyphenylalanine / analogs & derivatives*
  • Dihydroxyphenylalanine / chemistry
  • Hydrogen-Ion Concentration
  • Hydroxylation
  • Lysine / analogs & derivatives
  • Lysine / chemistry
  • Oxidation-Reduction
  • Phenols / chemistry*
  • Quinones / chemistry

Substances

  • 2-hydroxy-5-tert-butyl-1,4-benzoquinone
  • Benzoquinones
  • Phenols
  • Quinones
  • lysine tyrosylquinone
  • Dihydroxyphenylalanine
  • 6-hydroxydopa quinone
  • Copper
  • Amine Oxidase (Copper-Containing)
  • Lysine
  • butylphen