NDLI: Sulfur Oxygenation in Biomimetic Non-Heme Iron-Thiolate Complexes

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Tin(IV) and lead(IV) complexes with a tetradentate redox-active ligand

A tetrameric neptunyl(V) cluster supported by a Schiff base ligand

Sulfur Oxygenation in Biomimetic Non-Heme Iron-Thiolate Complexes

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Coordination of a chiral tin(II) cation bearing a bis(oxazoline) ligand with tetrahydrofuran derivatives

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Sulfur Oxygenation in Biomimetic Non-Heme Iron-Thiolate Complexes

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Mcquilken, Alison C. Goldberg, David P.
Description	Author Affiliation: McQuilken AC ( Department of Chemistry, The Johns Hopkins University, Baltimore, Maryland 21218, USA.)
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 [N(x)S(y)]-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 O(2) 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 O(2) 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 O(2) 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.
ISSN	14779226
e-ISSN	13645447
Journal	Dalton Trans.
Issue Number	36
Volume Number	41
Language	English
Publisher	Royal Society of Chemistry
Publisher Date	2012-08-28
Publisher Place	Great Britain (UK)
Access Restriction	Open
Subject Keyword	Biomimetic Materials Chemistry Coordination Complexes Ferric Compounds Ferrous Compounds Sulfhydryl Compounds Metabolism Catalytic Domain Crystallography, X-Ray Heme Hydro-Lyases Molecular Conformation Oxidoreductases Oxygen Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't
Content Type	Text
Resource Type	Article
Subject	Inorganic Chemistry

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