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Oxygenases: mechanisms and structural motifs for O-2 activation

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UNSPECIFIED (2001) Oxygenases: mechanisms and structural motifs for O-2 activation. [Journal Item]

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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 monooxygenases. 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.

Item Type: Journal Item
Subjects: Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
Journal or Publication Title: CURRENT OPINION IN CHEMICAL BIOLOGY
Publisher: CURRENT BIOLOGY LTD
ISSN: 1367-5931
Date: October 2001
Volume: 5
Number: 5
Number of Pages: 6
Page Range: pp. 550-555
Publication Status: Published
URI: http://wrap.warwick.ac.uk/id/eprint/11687

Data sourced from Thomson Reuters' Web of Knowledge

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