Abstract
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) |
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Pages (from-to) | 351-358 |
Number of pages | 8 |
Journal | Chemtracts |
Volume | 17 |
Issue number | 7 |
State | Published - Jul 2004 |
ASJC Scopus subject areas
- General Chemistry
- Biochemistry
- Molecular Biology