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Sulfur oxygenation in biomimetic non-heme iron–thiolate complexes

Sulfur oxygenation in biomimetic non-heme iron–thiolate complexes The S-oxygenation of cysteine with dioxygen to give cysteine sulfinic acid occurs at the non-heme iron active site of cysteine dioxygenase. Similar S-oxygenation events occur in other non-heme iron enzymes, including nitrile hydratase and isopenicillin N synthase, and these enzymes have inspired the development of a class of [NxSy]–Fe model complexes. Certain members of this class have provided some intriguing examples of S-oxygenation, and this article summarizes these results, focusing on the non-heme iron(ii/iii)–thiolate model complexes that are known to react with O2 or other O-atom transfer oxidants to yield sulfur oxygenates. Key aspects of the synthesis, structure, and reactivity of these systems are presented, along with any mechanistic information available on the oxygenation reactions. A number of iron(iii)–thiolate complexes react with O2 to give S-oxygenates, and the degree to which the thiolate sulfur donors are oxidized varies among the different complexes, depending upon the nature of the ligand, metal geometry, and spin state. The first examples of iron(ii)–thiolate complexes that react with O2 to give selective S-oxygenation are just emerging. Mechanistic information on these transformations is limited, with isotope labeling studies providing much of the current mechanistic data. The many questions that remain unanswered for both models and enzymes provide strong motivation for future work in this area. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Dalton Transactions Royal Society of Chemistry

Sulfur oxygenation in biomimetic non-heme iron–thiolate complexes

McQuilken, Alison C.; Goldberg, David P.
Dalton Transactions , Volume 41 (36) – Aug 28, 2012
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References (88)

Publisher
Royal Society of Chemistry
Copyright
This journal is © The Royal Society of Chemistry
ISSN
1477-9226
eISSN
1477-9234
DOI
10.1039/c2dt30806a
pmid
22814765
Publisher site
See Article on Publisher Site

Abstract

The S-oxygenation of cysteine with dioxygen to give cysteine sulfinic acid occurs at the non-heme iron active site of cysteine dioxygenase. Similar S-oxygenation events occur in other non-heme iron enzymes, including nitrile hydratase and isopenicillin N synthase, and these enzymes have inspired the development of a class of [NxSy]–Fe model complexes. Certain members of this class have provided some intriguing examples of S-oxygenation, and this article summarizes these results, focusing on the non-heme iron(ii/iii)–thiolate model complexes that are known to react with O2 or other O-atom transfer oxidants to yield sulfur oxygenates. Key aspects of the synthesis, structure, and reactivity of these systems are presented, along with any mechanistic information available on the oxygenation reactions. A number of iron(iii)–thiolate complexes react with O2 to give S-oxygenates, and the degree to which the thiolate sulfur donors are oxidized varies among the different complexes, depending upon the nature of the ligand, metal geometry, and spin state. The first examples of iron(ii)–thiolate complexes that react with O2 to give selective S-oxygenation are just emerging. Mechanistic information on these transformations is limited, with isotope labeling studies providing much of the current mechanistic data. The many questions that remain unanswered for both models and enzymes provide strong motivation for future work in this area.

Journal

Dalton Transactions – Royal Society of Chemistry

Published: Aug 28, 2012

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