Journal
ACCOUNTS OF CHEMICAL RESEARCH
Volume 39, Issue 8, Pages 558-566Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ar030204v
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Bacterial multicomponent monooxygenases (BMMs) catalyze the O-2-dependent hydroxylation of hydrocarbons at a carboxylate-bridged diiron center similar to those that occur in a variety of dimetallic oxygen-utilizing enzymes. BMMs have found numerous biodegradation and biocatalytic applications. Recent investigations have begun to reveal how BMMs perform their C-H bond activation chemistry and why these enzymes may be mechanistically different from other related diiron proteins. The structures of the BMM component proteins and of complexes between them provide insights into the tuning of the dinuclear iron center and the enzyme mechanism. Selected findings are compared and contrasted with the properties of other carboxylate-bridged diiron proteins, revealing common structural and functional themes.
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