Issue 36, 2012

Sulfur oxygenation in biomimetic non-heme iron–thiolate complexes

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.

Graphical abstract: Sulfur oxygenation in biomimetic non-heme iron–thiolate complexes

Article information

Article type
Perspective
Submitted
13 Apr 2012
Accepted
31 May 2012
First published
01 Jun 2012

Dalton Trans., 2012,41, 10883-10899

Sulfur oxygenation in biomimetic non-heme iron–thiolate complexes

A. C. McQuilken and D. P. Goldberg, Dalton Trans., 2012, 41, 10883 DOI: 10.1039/C2DT30806A

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements