Mechanism of extradiol aromatic ring-cleaving dioxygenases.
The extradiol aromatic ring-cleaving dioxygenases activate molecular oxygen by binding both O(2) and the catecholic substrate to a reduced active site metal, generally Fe(II). Progress has been made in understanding the mechanism of this reaction through the combined use of kinetic, computational, biomimetic, structural, and diagnostic chemical approaches. It appears that O(2) is activated by accepting an electron transferred from the substrate through the metal, thereby simultaneously activating oxygen and substrate for reaction with each other.
Lipscomb
John D
JD
Department of Biochemistry, Molecular Biology, and Biophysics, Center for Metals in Biocatalysis, University of Minnesota, Minneapolis, MN 55455, USA. Lipsc001@umn.edu
D000818:Animals; D001665:Binding Sites; D007501:Iron / Q000378:metabolism; D015394:Molecular Structure; D010084:Oxidation-Reduction; D010100:Oxygen / Q000378:metabolism; D010105:Oxygenases / Q000737:chemistry* / Q000378:metabolism*; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D007501:Iron; D010105:Oxygenases; C439587:extradiol dioxygenase; D010100:Oxygen