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Updated: Jul 6, 2026

Preparation of Polyoxometalate-based Photo-responsive Membranes for the Photo-activation of Manganese Oxide Catalysts
Published on: August 7, 2018
Dioxygen binds end-on to mononuclear copper in a precatalytic enzyme complex
Sean T Prigge1, Betty A Eipper, Richard E Mains
1Department of Microbiology and Molecular Immunology, The Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD, USA.
Researchers captured a key copper-dioxygen complex in the peptidylglycine-alpha-hydroxylating monooxygenase (PHM) enzyme. This structure reveals how oxygen activates for enzymatic reactions, offering insights into copper-containing enzymes.
Area of Science:
- Biochemistry
- Enzymology
- Structural Biology
Background:
- Copper active sites are crucial for enzymatic dioxygen activation.
- Understanding these mechanisms is key to various biological processes and biomimetic design.
Purpose of the Study:
- To elucidate the structure of a precatalytic copper-dioxygen complex in peptidylglycine-alpha-hydroxylating monooxygenase (PHM).
- To understand the role of dioxygen in the PHM reaction mechanism.
Main Methods:
- X-ray crystallography was used to determine the structure of the enzyme-dioxygen complex.
- Crystals of PHM were soaked with substrate and ascorbate in the presence of oxygen and then frozen.
Main Results:
- The structure of the copper-dioxygen complex was determined at 1.85-angstrom resolution.
- Oxygen was observed to bind to copper with an end-on geometry within the PHM active site.
Conclusions:
- The determined structure suggests direct involvement of dioxygen in electron transfer and hydrogen abstraction.
- These findings have implications for understanding other copper-oxygen activating enzymes and designing biomimetic catalysts.
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