Bugg_2001_Curr.Opin.Chem.Biol_5_550

Reference

Title : Oxygenases: mechanisms and structural motifs for O(2) activation - Bugg_2001_Curr.Opin.Chem.Biol_5_550
Author(s) : Bugg TD
Ref : Curr Opin Chemical Biology , 5 :550 , 2001
Abstract :

Recent structural and mechanistic analysis of oxygenase enzymes together with the study of biomimetic model reactions have provided new insights into the catalytic mechanisms of oxygenase-catalysed reactions. High-valent iron-oxo intermediates have been implicated in heme- and pterin-dependent mono-oxygenases. Structural motifs have been identified for binding of non-heme iron(II) (His,His,Glu) and iron(III) (His(2)Tyr(2)) in non-heme-dependent dioxygenases, but additional factors influencing the choice of reaction pathway are emerging from model studies.

PubMedSearch : Bugg_2001_Curr.Opin.Chem.Biol_5_550
PubMedID: 11578928

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Citations formats

Bugg TD (2001)
Oxygenases: mechanisms and structural motifs for O(2) activation
Curr Opin Chemical Biology 5 :550

Bugg TD (2001)
Curr Opin Chemical Biology 5 :550