ArticleThe journal of physical chemistry. A2012
Mechanism of S-oxygenation by a cysteine dioxygenase model complex.
Article in The journal of physical chemistry. A, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Biosynthesis of antibiotics with sulfonamide and azaindane moieties.The Journal of antibiotics · 2025Review
- Keratinous bioresources: their generation, microbial degradation, and value enhancement for biotechnological applications.World journal of microbiology & biotechnology · 2025Review
- Unusual cysteine modifications in natural product biosynthesis.RSC chemical biology · 2024Review
- Superoxide Oxidation by a Thiolate-Ligated Iron Complex and Anion Inhibition.Inorganic chemistry · 2021Article
- Nonheme iron-thiolate complexes as structural models of sulfoxide synthase active sites.Dalton transactions (Cambridge, England : 2003) · 2020Article
- Enhancing Tris(pyrazolyl)borate-Based Models of Cysteine/Cysteamine Dioxygenases through Steric Effects: Increased Reactivities, Full Product Characterization and Hints to Initial Superoxide Formation.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020Article
- Metal-Assisted Oxo Atom Addition to an Fe(III) Thiolate.Journal of the American Chemical Society · 2017Article
- Synthesis, X-ray Structures, Electronic Properties, and OInorganic chemistry · 2016Article
- Mono- and binuclear non-heme iron chemistry from a theoretical perspective.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016Review
- Photoinitiated Reactivity of a Thiolate-Ligated, Spin-Crossover Nonheme {FeNO}(7) Complex with Dioxygen.Journal of the American Chemical Society · 2016Article
- Structures of Arg- and Gln-type bacterial cysteine dioxygenase homologs.Protein science : a publication of the Protein Society · 2015Article
- Dramatically accelerated selective oxygen-atom transfer by a nonheme iron(IV)-oxo complex: tuning of the first and second coordination spheres.Journal of the American Chemical Society · 2014Article
- Preparation of non-heme {FeNO}7 models of cysteine dioxygenase: sulfur versus nitrogen ligation and photorelease of nitric oxide.Journal of the American Chemical Society · 2013Article
- Synthesis and ligand non-innocence of thiolate-ligated (N4S) Iron(II) and nickel(II) bis(imino)pyridine complexes.Inorganic chemistry · 2013Article
- Cysteine dioxygenase structures from pH4 to 9: consistent cys-persulfenate formation at intermediate pH and a Cys-bound enzyme at higher pH.Journal of molecular biology · 2013Article
- Sulfur oxygenation in biomimetic non-heme iron-thiolate complexes.Dalton transactions (Cambridge, England : 2003) · 2012Article
- Axial and equatorial ligand effects on biomimetic cysteine dioxygenase model complexes.Organic & biomolecular chemistry · 2012Article
- Addition of dioxygen to an N4S(thiolate) iron(II) cysteine dioxygenase model gives a structurally characterized sulfinato-iron(II) complex.Journal of the American Chemical Society · 2012Article
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4 authors.
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Abstract
In this work, we present the first computational study on a biomimetic cysteine dioxygenase model complex, [Fe(II)(LN(3)S)](+), in which LN(3)S is a tetradentate ligand with a bis(imino)pyridyl scaffold and a pendant arylthiolate group. The reaction mechanism of sulfur dioxygenation with O(2) was examined by density functional theory (DFT) methods and compared with results obtained for cysteine dioxygenase. The reaction proceeds via multistate reactivity patterns on competing singlet, triplet, and quintet spin state surfaces. The reaction mechanism is analogous to that found for cysteine dioxygenase enzymes (Kumar, D.; Thiel, W.; de Visser, S. P. J. Am. Chem. Soc. 2011, 133, 3869-3882); hence, the computations indicate that this complex can closely mimic the enzymatic process. The catalytic mechanism starts from an iron(III)-superoxo complex and the attack of the terminal oxygen atom of the superoxo group on the sulfur atom of the ligand. Subsequently, the dioxygen bond breaks to form an iron(IV)-oxo complex with a bound sulfenato group. After reorganization, the second oxygen atom is transferred to the substrate to give a sulfinic acid product. An alternative mechanism involving the direct attack of dioxygen on the sulfur, without involving any iron-oxygen intermediates, was also examined. Importantly, a significant energetic preference for dioxygen coordinating to the iron center prior to attack at sulfur was discovered and serves to elucidate the function of the metal ion in the reaction process. The computational results are in good agreement with experimental observations, and the differences and similarities of the biomimetic complex and the enzymatic cysteine dioxygenase center are highlighted.
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