Correlating structure with function in bacterial multicomponent monooxygenases and related diiron proteins.
Bacterial multicomponent monooxygenases (BMMs) catalyze the O2-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.
Sazinsky
Matthew H
MH
Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
Lippard
Stephen J
SJ
D001419:Bacteria / Q000201:enzymology*; D001665:Binding Sites; D006860:Hydrogen Bonding; D007501:Iron / Q000378:metabolism*; D008667:Metalloproteins / Q000378:metabolism*; D006899:Mixed Function Oxygenases / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D010640:Phenothiazines / Q000378:metabolism; D020836:Protein Structure, Quaternary; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism; D013329:Structure-Activity Relationship
D008667:Metalloproteins; D010640:Phenothiazines; D021122:Protein Subunits; D007501:Iron; D006899:Mixed Function Oxygenases; C009469:thionine