Iron-catalyzed olefin cis-dihydroxylation using a bio-inspired N,N, O-ligand

Paul D. Oldenburg, Albert A. Shteinman, Lawrence Que

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102 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)15672-15673
Number of pages2
JournalJournal of the American Chemical Society
Volume127
Issue number45
DOIs
StatePublished - Nov 16 2005

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