Dioxygen-activating bio-inorganic model complexes

The study of model compounds continues to significantly contribute to our understanding of the role of transition metals at the active sites of enzymes. Recent advances in the field include the use of mimics for enzymes that activate dioxygen, as dioxygen is not only manipulated in nature but also h...

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Published inCurrent opinion in chemical biology Vol. 3; no. 2; pp. 168 - 175
Main Authors Liang, Hong-Chang, Dahan, Mazal, Karlin, Kenneth D
Format Journal Article
LanguageEnglish
Published England Elsevier Ltd 01.04.1999
Subjects
Copper - metabolism
Hemerythrin - metabolism
Models, Chemical
Models, Molecular
Oxidoreductases - metabolism
Oxygen - metabolism
Oxygenases - metabolism
GO
Hr
XYL
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Summary:The study of model compounds continues to significantly contribute to our understanding of the role of transition metals at the active sites of enzymes. Recent advances in the field include the use of mimics for enzymes that activate dioxygen, as dioxygen is not only manipulated in nature but also has industrial significance in metal-catalyzed oxidations of organics. Copper, nonheme and heme iron coordination complexes have been used to mimic reversible dioxygen-binding by the three classes of blood-oxygen carriers — hemocyanin, hemerythrin and hemoglobin/myoglobin — while functional mimics of oxygenases and oxidases with copper and iron have also provided key insights into important dioxygen activation processes.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-3
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ObjectType-Review-1
ISSN:1367-5931
1879-0402
DOI:10.1016/S1367-5931(99)80029-5