ArticleBiochemistry2014
Spectroscopic and computational investigation of iron(III) cysteine dioxygenase: implications for the nature of the putative superoxo-Fe(III) intermediate.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- An mRNA-display derived cyclic peptide scaffold reveals the substrate binding interactions of an N-terminal cysteine oxidase.Nature communications · 2025Article
- Influence of the second coordination sphere on OJournal of inorganic biochemistry · 2025Article
- Association of Single Nucleotide Polymorphisms in Cysteamine Dioxygenase Gene with Taurine Content in Oyster Crassostrea gigas.Marine biotechnology (New York, N.Y.) · 2025Article
- Kinetic and Spectroscopic Investigation of the Y157F and C93G/Y157F Variants of Cysteine Dioxygenase: Dissecting the Roles of the Second-Sphere Residues C93 and Y157.Biochemistry · 2024Article
- Unusual cysteine modifications in natural product biosynthesis.RSC chemical biology · 2024Review
- A Nonheme Iron(III) Superoxide Complex Leads to Sulfur Oxygenation.Journal of the American Chemical Society · 2024Article
- Spectroscopic analysis of the mammalian enzyme cysteine dioxygenase.Methods in enzymology · 2023Article
- Electronic Structure and Reactivity of Dioxygen-Derived Aliphatic Thiolate-Ligated Fe-Peroxo and Fe(IV) Oxo Compounds.Journal of the American Chemical Society · 2022Article
- Spectroscopic investigation of iron(III) cysteamine dioxygenase in the presence of substrate (analogs): implications for the nature of substrate-bound reaction intermediates.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2021Article
- Increasing reactivity by incorporating π-acceptor ligands into coordinatively unsaturated thiolate-ligated iron(II) complexes.Inorganica chimica acta · 2021Article
- Superoxide Oxidation by a Thiolate-Ligated Iron Complex and Anion Inhibition.Inorganic chemistry · 2021Article
- Spectroscopic Investigation of Cysteamine Dioxygenase.Biochemistry · 2020Article
- Spectroscopic and Computational Comparisons of Thiolate-Ligated Ferric Nonheme Complexes to Cysteine Dioxygenase: Second-Sphere Effects on Substrate (Analogue) Positioning.Inorganic chemistry · 2019Article
- Spectroscopic and Electronic Structure Study of ETHE1: Elucidating the Factors Influencing Sulfur Oxidation and Oxygenation in Mononuclear Nonheme Iron Enzymes.Journal of the American Chemical Society · 2018Article
- Use of a Tyrosine Analogue To Modulate the Two Activities of a Nonheme Iron Enzyme OvoA in Ovothiol Biosynthesis, Cysteine Oxidation versus Oxidative C-S Bond Formation.Journal of the American Chemical Society · 2018Article
- Go it alone: four-electron oxidations by mononuclear non-heme iron enzymes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2017Review
- Structure-Based Insights into the Role of the Cys-Tyr Crosslink and Inhibitor Recognition by Mammalian Cysteine Dioxygenase.Journal of molecular biology · 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
- Non-chemical proton-dependent steps prior to O2-activation limit Azotobacter vinelandii 3-mercaptopropionic acid dioxygenase (MDO) catalysis.Archives of biochemistry and biophysics · 2016Article
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3 authors.
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Abstract
Cysteine dioxygenase (CDO) is a mononuclear, non-heme iron-dependent enzyme that converts exogenous cysteine (Cys) to cysteine sulfinic acid using molecular oxygen. Although the complete catalytic mechanism is not yet known, several recent reports presented evidence for an Fe(III)-superoxo reaction intermediate. In this work, we have utilized spectroscopic and computational methods to investigate the as-isolated forms of CDO, as well as Cys-bound Fe(III)CDO, both in the absence and presence of azide (a mimic of superoxide). An analysis of our electronic absorption, magnetic circular dichroism, and electron paramagnetic resonance data of the azide-treated as-isolated forms of CDO within the framework of density functional theory (DFT) computations reveals that azide coordinates directly to the Fe(III), but not the Fe(II) center. An analogous analysis carried out for Cys-Fe(III)CDO provides compelling evidence that at physiological pH, the iron center is six coordinate, with hydroxide occupying the sixth coordination site. Upon incubation of this species with azide, the majority of the active sites retain hydroxide at the iron center. Nonetheless, a modest perturbation of the electronic structure of the Fe(III) center is observed, indicating that azide ions bind near the active site. Additionally, for a small fraction of active sites, azide displaces hydroxide and coordinates directly to the Cys-bound Fe(III) center to generate a low-spin (S = (1)/2) Fe(III) complex. In the DFT-optimized structure of this complex, the central nitrogen atom of the azide moiety lies within 3.12 Å of the cysteine sulfur. A similar orientation of the superoxide ligand in the putative Fe(III)-superoxo reaction intermediate would promote the attack of the distal oxygen atom on the sulfur of substrate Cys.
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