Oxygenases: mechanisms and structural motifs for O-2 activation
UNSPECIFIED (2001) Oxygenases: mechanisms and structural motifs for O-2 activation. CURRENT OPINION IN CHEMICAL BIOLOGY, 5 (5). pp. 550-555. ISSN 1367-5931Full text not available from this repository.
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|
|Number of Pages:||6|
|Page Range:||pp. 550-555|
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