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Dalton Transactions Vol - 0 Issue - 5

myo-Inositol oxygenase: a radical new pathway for O₂ and C–H activation at a nonheme diiron cluster

Content Provider	Royal Society of Chemistry (RSC)
Author	Diao, Yinghui Bollinger, J. Martin Krebs, Carsten Xing, Gang Matthews, Megan L.
Copyright Year	2009
Abstract	The enzyme myo-inositol oxygenase (MIOX) catalyzes conversion of myo-inositol (cyclohexan-1,2,3,5/4,6-hexa-ol or MI) to D-glucuronate (DG), initiating the only known pathway in humans for catabolism of the carbon skeleton of cell-signaling inositol (poly)phosphates and phosphoinositides. Recent kinetic, spectroscopic and crystallographic studies have shown that the enzyme activates its substrates, MI and O2, at a carboxylate-bridged nonheme diiron(II/III) cluster, making it the first of many known nonheme diiron oxygenases to employ the mixed-valent form of its cofactor. Evidence suggests that: (1) the Fe(III) site coordinates MI via its C1 and C6 hydroxyl groups; (2) the Fe(II) site reversibly coordinates O2 to produce a superoxo-diiron(III/III) intermediate; and (3) the pendant oxygen atom of the superoxide ligand abstracts hydrogen from C1 to initiate the unique C–C-bond-cleaving, four-electron oxidation reaction. This review recounts the studies leading to the recognition of the novel cofactor requirement and catalytic mechanism of MIOX and forecasts how remaining gaps in our understanding might be filled by additional experiments.
Starting Page	905
Ending Page	914
Page Count	10
File Format	HTM / HTML PDF
ISSN	14779226
Volume Number	0
Issue Number	6
Journal	Dalton Transactions
DOI	10.1039/b811885j
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Enzyme Inositol Catalysis Glucuronic acid Catabolism Carbon Allotropes of oxygen Cofactor (biochemistry) Hydroxy group Superoxide Ligand
Content Type	Text
Resource Type	Article
Subject	Inorganic Chemistry

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myo-Inositol Oxygenase: a Radical New Pathway for O2 and C-H Activation at a Nonheme Diiron Cluster

myo-Inositol Oxygenase: a Radical New Pathway for $O_{2}$ and C-H Activation at a Nonheme Diiron Cluster

Efficient expression of myo-inositol oxygenase in Escherichia coli and application for conversion of myo-inositol to glucuronic acid

Evidence for C–H cleavage by an iron–superoxide complex in the glycol cleavage reaction catalyzed by myo-inositol oxygenase

Current challenges of modeling diiron enzyme active sites for dioxygen activation by biomimetic synthetic complexes

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DNA binding and oxidative DNA cleavage activity of (μ-oxo)diiron(iii) complexes in visible light

myo-Inositol oxygenase: a radical new pathway for O₂ and C–H activation at a nonheme diiron cluster

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myo-Inositol oxygenase: a radical new pathway for O2 and C–H activation at a nonheme diiron cluster

myo-Inositol oxygenase: a radical new pathway for O₂ and C–H activation at a nonheme diiron cluster