Iron-catalyzed olefin cis-dihydroxylation using a bio-inspired N,N,O-ligand.
Nature has evolved enzymes that carry out the cis-dihydroxylation of C=C bonds in the biodegradation of arenes in the environment. These enzymes, called Rieske dioxygenases, have mononuclear iron centers coordinated to a 2-His-1-carboxylate facial triad motif that has emerged as a common structural element among many nonheme iron enzymes. In contrast, olefin cis-dihydroxylation is conveniently carried out by OsO4 and related species in synthetic procedures. To develop more environmentally benign strategies for carrying out these transformations, we have designed Ph-DPAH [(di-(2-pyridyl)methyl)benzamide], a tridentate ligand that mimics the facial N,N,O site of the mononuclear iron center in the Rieske dioxygenases. Its iron(II) complex has been found to catalyze olefin cis-dihydroxylation almost exclusively and with high H2O2 conversion efficiency on a wide range of substrates. and 18O labeling experiments suggest the participation of an FeV oxidant.
Oldenburg
Paul D
PD
Department of Chemistry and Center for Metals in Biocatalysis, University of Minnesota, Minneapolis, Minnesota 55455, USA.
Shteinman
Albert A
AA
Que
Lawrence
L
D000475:Alkenes / Q000737:chemistry*; D002384:Catalysis; D006900:Hydroxylation; D007501:Iron / Q000737:chemistry*; D008024:Ligands; D015394:Molecular Structure
D000475:Alkenes; D008024:Ligands; D007501:Iron