Dioxygen binds end-on to mononuclear copper in a precatalytic enzyme complex

S. T. Prigge, B. A. Eipper, R. E. Mains, L. M. Amzel, Julia E. Salas, Edward I. Solomon

Research output: Contribution to journalReview articlepeer-review


In this work, the authors present the first crystal structure of a noncoupled binuclear copper site in an enzyme with substrate and dioxygen bound. The precatalytic complex of PHM with dioxygen was trapped by utilizing a radical-resistant substrate (IYT) which was designed to slow the hydrogen atom abstraction reaction of PHM. This structure was obtained at 1.85 A resolution and shows an end-on η 1 bound dioxygen intermediate on the PHM Cu B site. The structure of this complex provides insight into the enzymatic activation of dioxygen by a single copper center and helps to elucidate the molecular mechanisms of the noncoupled binuclear copper monooxygenases DβM and PHM.

Original languageEnglish (US)
Pages (from-to)351-358
Number of pages8
Issue number7
StatePublished - Jul 1 2004
Externally publishedYes

ASJC Scopus subject areas

  • General Chemistry
  • Biochemistry
  • Molecular Biology


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