| People | Locations | Statistics |
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| Naji, M. |
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| Motta, Antonella |
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| Aletan, Dirar |
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| Mohamed, Tarek |
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| Ertürk, Emre |
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| Taccardi, Nicola |
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| Kononenko, Denys |
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| Petrov, R. H. | Madrid |
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| Alshaaer, Mazen | Brussels |
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| Bih, L. |
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| Casati, R. |
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| Muller, Hermance |
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| Kočí, Jan | Prague |
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| Šuljagić, Marija |
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| Kalteremidou, Kalliopi-Artemi | Brussels |
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| Azam, Siraj |
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| Ospanova, Alyiya |
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| Blanpain, Bart |
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| Ali, M. A. |
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| Popa, V. |
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| Rančić, M. |
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| Ollier, Nadège |
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| Azevedo, Nuno Monteiro |
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| Landes, Michael |
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| Rignanese, Gian-Marco |
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De Visser, Samuel P.
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Topics
Publications (9/9 displayed)
- 2023Defluorination of fluorophenols by a nonheme iron(IV)‐oxo species: observation of a new intermediate along the reactioncitations
- 2021Biodegradation of herbicides by a plant nonheme iron dioxygenase: mechanism and selectivity of substrate analoguescitations
- 2018Mechanistic insight on the activity and substrate selectivity of nonheme iron dioxygenasescitations
- 2017A high-valent non heme μ-oxo MnIV dimer generated from a thiolate-bound MnII complex and O2citations
- 2017The Role of Nonheme Transition Metal-Oxo, -Peroxo, and -Superoxo Intermediates in Enzyme Catalysis and Reactions of Bioinspired Complexescitations
- 2017The Role of Nonheme Transition Metal-Oxo, -Peroxo and -Superoxo Intermediates in Enzyme Catalysis and Reactions of Bio-Inspired Complexes.
- 2011Theoretical study on the mechanism of the oxygen activation process in cysteine dioxygenase enzymescitations
- 2006The axial ligand effect of oxo-iron porphyrin catalysts. How does chloride compare to thiolate?citations
- 2006What external perturbations influence the electronic properties of catalase compound I?citations
Places of action
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article
Theoretical study on the mechanism of the oxygen activation process in cysteine dioxygenase enzymes
Abstract
Cysteine dioxygenase (CDO) is a vital enzyme for human health involved in the biodegradation of toxic cysteine and thereby regulation of the cysteine concentration in the body. The enzyme belongs to the group of nonheme iron dioxygenases and utilizes molecular oxygen to transfer two oxygen atoms to cysteinate to form cysteine sulfinic acid products. The mechanism for this reaction is currently disputed, with crystallographic studies implicating a persulfenate intermediate in the catalytic cycle. To resolve the dispute we have performed quantum mechanics/molecular mechanics (QM/MM) calculations on substrate activation by CDO enzymes using an enzyme monomer and a large QM active region. We find a stepwise mechanism, whereby the distal oxygen atom of the iron(II)-superoxo complex attacks the sulfur atom of cysteinate to form a ring structure, followed by dioxygen bond breaking and the formation of a sulfoxide bound to an iron(IV)-oxo complex. A sulfoxide rotation precedes the second oxygen atom transfer to the substrate to give cysteine sulfinic acid products. The reaction takes place on several low-lying spin-state surfaces via multistate reactivity patterns. It starts in the singlet ground state of the iron(II)-superoxo reactant and then proceeds mainly on the quintet and triplet surfaces. The initial and rate-determining attack of the superoxo group on the cysteinate sulfur atom involves a spin-state crossing from singlet to quintet. We have also investigated an alternative mechanism via a persulfenate intermediate, with a realignment of hydrogen bonding interactions in the substrate binding pocket. However, this alternative mechanism of proximal oxygen atom attack on the sulfur atom of cysteinate is computed to be a high-energy pathway, and therefore, the persulfenate intermediate is unlikely to participate in the catalytic cycle of CDO enzymes. © 2011 American Chemical Society.