Mimicking the intradiol catechol cleavage activity of catechol dioxygenase by high-spin iron(III) complexes of a new class of a facially bound [N 2O] ligand

Manas K. Panda, Alex John, Mobin M. Shaikh, Prasenjit Ghosh

Research output: Contribution to journalArticlepeer-review

19 Scopus citations

Abstract

A series of high-spin iron(III) complexes, {N-R-2-[(pyridin-2-ylmethyl) amino]acetamide}FeCl3 [R = mesityl (1b), 2,6-Et2C 6H3 (2b), and 2,6-i-Pr2C6H 3 (3b)], that functionally emulate the intradiol catechol dioxygenase enzyme are reported. In particular, these enzyme mimics, 1b, 2b, and 3b, which utilized molecular oxygen in carrying out the intradiol catechol cleavage of 3,5-di-tert-butylcatechol with high regioselectivity (ca. 81-85%) at room temperature under ambient conditions, were designed by employing a new class of a facially bound [N2O] ligand, namely, N-R-2-[(pyridin-2-ylmethyl) amino]acetamide [R = mesityl (1a), 2,6-Et2C6H3 (2a), and 2,6-i-Pr2C6H3 (3a)]. The density functional theory studies revealed that the intradiol catechol cleavage reaction proceeded by an iron(III) peroxo intermediate that underwent 1,2-Criegee rearrangement to yield the intradiol catechol cleaved products analogous to the native enzyme.

Original languageEnglish (US)
Pages (from-to)11847-11856
Number of pages10
JournalInorganic chemistry
Volume47
Issue number24
DOIs
StatePublished - 2008
Externally publishedYes

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