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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. CURRENT OPINION IN CHEMICAL BIOLOGY, 5 (5). pp. 550-555.
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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 | ||||
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Subjects: | Q Science > QD Chemistry Q Science > QH Natural history > QH301 Biology |
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Journal or Publication Title: | CURRENT OPINION IN CHEMICAL BIOLOGY | ||||
Publisher: | CURRENT BIOLOGY LTD | ||||
ISSN: | 1367-5931 | ||||
Official Date: | October 2001 | ||||
Dates: |
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Volume: | 5 | ||||
Number: | 5 | ||||
Number of Pages: | 6 | ||||
Page Range: | pp. 550-555 | ||||
Publication Status: | Published |
Data sourced from Thomson Reuters' Web of Knowledge
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