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Oxygenases: mechanisms and structural motifs for O(2) activation
1Department of Chemistry, University of Warwick, Coventry CV4 7AL, UK. mssgv@warwick.ac.uk
Current Opinion in Chemical Biology
|October 2, 2001
Summary
New insights into oxygenase enzymes reveal high-valent iron-oxo intermediates in heme- and pterin-dependent reactions. Model studies are uncovering factors influencing reaction pathways in non-heme dioxygenases.
Area of Science:
- Biochemistry
- Enzymology
- Bioinorganic Chemistry
Background:
- Oxygenase enzymes catalyze crucial biological oxidation reactions.
- High-valent iron-oxo intermediates are key mechanistic features in heme- and pterin-dependent mono-oxygenases.
- Understanding non-heme iron coordination is vital for dioxygenase mechanisms.
Purpose of the Study:
- To provide new insights into the catalytic mechanisms of oxygenase-catalyzed reactions.
- To identify structural motifs for non-heme iron binding in dioxygenases.
- To explore factors influencing reaction pathway selection in oxygenase models.
Main Methods:
- Structural and mechanistic analysis of oxygenase enzymes.
- Study of biomimetic model reactions.
- Identification of conserved structural motifs for metal ion binding.
Main Results:
- High-valent iron-oxo intermediates implicated in heme- and pterin-dependent mono-oxygenases.
- Structural motifs (His,His,Glu) for non-heme iron(II) and (His(2)Tyr(2)) for iron(III) identified in dioxygenases.
- Emerging evidence from model studies suggests additional factors influence oxygenase reaction pathways.
Conclusions:
- Structural and mechanistic studies offer significant insights into oxygenase catalysis.
- The identification of specific iron-binding motifs advances our understanding of non-heme dioxygenases.
- Biomimetic models are crucial for elucidating the complex factors governing oxygenase reaction selectivity.