Dioxygen activation by biomimetic iron complexes of α-keto acids and α-hydroxy acids

Tapan Kanti Paine; Lawrence Que

doi:10.1007/430-2014-144

Dioxygen activation by biomimetic iron complexes of α-keto acids and α-hydroxy acids

Tapan Kanti Paine, Lawrence Que

Chemistry (Twin Cities)

Research output: Chapter in Book/Report/Conference proceeding › Chapter

16 Scopus citations

Abstract

A subset of the large family of nonheme iron oxygenases carries out the oxidative decarboxylation of α-ketocarboxylate and α- hydroxycarboxylate substrates in the presence of O₂. Iron complexes of α-ketocarboxylates and α-hydroxycarboxylates supported by tridentate and tetradentate ligands have been synthesized to act as functional models for these enzymes, and several have been structurally characterized. From studies of these model complexes and their reactivity toward various probe substrates, insights into the reaction mechanisms have been obtained, where iron(III)-superoxo and iron(IV)-oxo species have been implicated as key oxidants.

Original language	English (US)
Title of host publication	Molecular Design in Inorganic Biochemistry
Publisher	Springer Verlag
Pages	39-56
Number of pages	18
ISBN (Print)	9783662435984
DOIs	https://doi.org/10.1007/430-2014-144
State	Published - 2014

Publication series

Name	Structure and Bonding
Volume	160
ISSN (Print)	0081-5993
ISSN (Electronic)	1616-8550

Bibliographical note

Funding Information:
The authors are supported respectively by the DST, Govt. of India (Project: SR/S1/IC-51/2010), and the US National Science Foundation (Grant CHE-1058248). We thank Dr. Caleb Allpress for a careful reading of the final manuscript.

Keywords

Biomimetic complexes
Dioxygen
Iron
α-Hydroxy acids
α-Keto acids

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title = "Dioxygen activation by biomimetic iron complexes of α-keto acids and α-hydroxy acids",

abstract = "A subset of the large family of nonheme iron oxygenases carries out the oxidative decarboxylation of α-ketocarboxylate and α- hydroxycarboxylate substrates in the presence of O2. Iron complexes of α-ketocarboxylates and α-hydroxycarboxylates supported by tridentate and tetradentate ligands have been synthesized to act as functional models for these enzymes, and several have been structurally characterized. From studies of these model complexes and their reactivity toward various probe substrates, insights into the reaction mechanisms have been obtained, where iron(III)-superoxo and iron(IV)-oxo species have been implicated as key oxidants.",

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author = "Paine, {Tapan Kanti} and Lawrence Que",

note = "Funding Information: The authors are supported respectively by the DST, Govt. of India (Project: SR/S1/IC-51/2010), and the US National Science Foundation (Grant CHE-1058248). We thank Dr. Caleb Allpress for a careful reading of the final manuscript.",

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AU - Paine, Tapan Kanti

AU - Que, Lawrence

N1 - Funding Information: The authors are supported respectively by the DST, Govt. of India (Project: SR/S1/IC-51/2010), and the US National Science Foundation (Grant CHE-1058248). We thank Dr. Caleb Allpress for a careful reading of the final manuscript.

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N2 - A subset of the large family of nonheme iron oxygenases carries out the oxidative decarboxylation of α-ketocarboxylate and α- hydroxycarboxylate substrates in the presence of O2. Iron complexes of α-ketocarboxylates and α-hydroxycarboxylates supported by tridentate and tetradentate ligands have been synthesized to act as functional models for these enzymes, and several have been structurally characterized. From studies of these model complexes and their reactivity toward various probe substrates, insights into the reaction mechanisms have been obtained, where iron(III)-superoxo and iron(IV)-oxo species have been implicated as key oxidants.

AB - A subset of the large family of nonheme iron oxygenases carries out the oxidative decarboxylation of α-ketocarboxylate and α- hydroxycarboxylate substrates in the presence of O2. Iron complexes of α-ketocarboxylates and α-hydroxycarboxylates supported by tridentate and tetradentate ligands have been synthesized to act as functional models for these enzymes, and several have been structurally characterized. From studies of these model complexes and their reactivity toward various probe substrates, insights into the reaction mechanisms have been obtained, where iron(III)-superoxo and iron(IV)-oxo species have been implicated as key oxidants.

KW - Biomimetic complexes

KW - Dioxygen

KW - Iron

KW - α-Hydroxy acids

KW - α-Keto acids

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BT - Molecular Design in Inorganic Biochemistry

PB - Springer Verlag

ER -

Dioxygen activation by biomimetic iron complexes of α-keto acids and α-hydroxy acids

Abstract

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Bibliographical note

Keywords

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