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 language||English (US)|
|Number of pages||8|
|State||Published - Jul 1 2004|
ASJC Scopus subject areas
- Molecular Biology