Mimicking the Intradiol Catechol Cleavage Activity of Catechol Dioxygenase by High-Spin Iron(III) Complexes of a New Class of a Facially Bound [N(2)O] Ligand
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Title |
Mimicking the Intradiol Catechol Cleavage Activity of Catechol Dioxygenase by High-Spin Iron(III) Complexes of a New Class of a Facially Bound [N(2)O] Ligand
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Creator |
PANDA, MK
JOHN, A SHAIKH, MM GHOSH, P |
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Subject |
nonheme iron enzymes
functional models protocatechuate 3,4-dioxygenase crystal-structures cleaving dioxygenases tridentate ligands catalytic-activity substrate complex binding-site 3n ligands |
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Description |
A series of high-spin iron(III) complexes, {N-R-2-[(pyridin-2-ylmethyl)amino]acetamide}FeCl(3) [R = mesityl (1b), 2,6-Et(2)C(6)H(3) (2b), and 2,6-i-Pr(2)C(6)H(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 [N(2)O] ligand, namely, N-R-2-[(pyridin-2-ylmethyl)amino]acetamide [R = mesityl (1a), 2,6-Et(2)C(6)H(3) (2a), and 2,6-i-Pr(2)C(6)H(3) (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.
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Publisher |
AMER CHEMICAL SOC
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Date |
2011-07-14T11:58:51Z
2011-12-26T12:48:22Z 2011-12-27T05:34:41Z 2011-07-14T11:58:51Z 2011-12-26T12:48:22Z 2011-12-27T05:34:41Z 2008 |
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Type |
Article
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Identifier |
INORGANIC CHEMISTRY, 47(24), 11847-11856
0020-1669 http://dx.doi.org/10.1021/ic801576f http://dspace.library.iitb.ac.in/xmlui/handle/10054/3947 http://hdl.handle.net/10054/3947 |
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Language |
en
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