Dioxygen Binds End-On to Mononuclear Copper in a Precatalytic Enzyme Complex

Sean T. Prigge, Betty A. Eipper, Richard E. Mains, L. Mario Amzel

Research output: Contribution to journalArticlepeer-review

326 Scopus citations


Copper active sites play a major role in enzymatic activation of dioxygen. We trapped the copper-dioxygen complex in the enzyme peptidylglycine-alpha-hydroxylating monooxygenase (PHM) by freezing protein crystals that had been soaked with a slow substrate and ascorbate in the presence of oxygen. The x-ray crystal structure of this precatalytic complex, determined to 1.85-angstrom resolution, shows that oxygen binds to one of the coppers in the enzyme with an end-on geometry. Given this structure, it is likely that dioxygen is directly involved in the electron transfer and hydrogen abstraction steps of the PHM reaction. These insights may apply to other copper oxygen-activating enzymes, such as dopamine beta-monooxygenase, and to the design of biomimetic complexes.

Original languageEnglish (US)
Pages (from-to)864-867
Number of pages4
Issue number5672
StatePublished - May 7 2004

ASJC Scopus subject areas

  • General


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