Evaluation of sulfur, selenium and tellurium catalysts with antioxidant potential

Giles, Gregory I.; Fry, Fiona H.; Tasker, Karen M.; Holme, Andrea L.; Peers, Chris; Green, Kim N.; Klotz, Lars‐Oliver; Sies, Helmut; Jacob, Claus

doi:10.1039/b308117f

Cited by 75 publications

(50 citation statements)

References 42 publications

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“…[37] The interaction of selenium (and tellurium) compounds with MT and GSH reveals a potential role for these in the development of novel therapeutic agents with zinc-releasing and antioxidant properties. [38,39] Specifically, selenium may be incorporated into proteins in the form of selenocysteine (Sec) and nonspecifically as selenomethionine. [40] It may therefore be possible to design and synthesize therapeutic agents and enzymes in which sulfur atoms are replaced by Se.…”

Section: Involvement Of Seleniummentioning

confidence: 99%

The Metallothionein/Thionein System: An Oxidoreductive Metabolic Zinc Link

2008

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Metallothioneins (MTs) were discovered more than 50 years ago and identified as low‐molecular weight, sulfhydryl‐rich proteins that were subsequently found to bind zinc predominantly. The binding of seemingly redox inactive zinc ions allows MT to play a central role in oxidoreductive cellular metabolism, cellular zinc distribution and homeostasis. In this interpretive study, we discuss the interaction of MT with physiologically relevant molecules and its effect on zincthiolate bonds. These interactions are linked to recent progress in the functional role of MT in cellular zinc transport, energy production, and protection of the organism against oxidative stress and neurodegenerative diseases.

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Section: Involvement Of Seleniummentioning

confidence: 99%

The Metallothionein/Thionein System: An Oxidoreductive Metabolic Zinc Link

2008

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“…Therefore, inhibition of the PN-mediated nitration and oxidation reaction is very essential. Sies et al, have reported several sulphur and selenium containing small molecules which are efficient inhibitor of PN-mediated nitration and oxidation reactions [37]. As many of the selenides and spirodiazaselenuranes react effectively with peroxides, we extended our work to investigate the effect of different substituents on the PN-scavenging antioxidant activity.…”

Section: Inhibition Of Peroxynitrite-mediated Nitration and Oxidationmentioning

confidence: 98%

“…The compound was purified in column chromatography using petroleum ether and ethyl acetate as eluents. Yield: 82%, (37): To a stirred solution of 36 (0.13 mmol) in dry CH2Cl2 (5 mL), hydrogen peroxide (0.13 mmol) was added. The reaction mixture was stirred for 4 h at room temperature.…”

Section: General Synthesis Of Spirodiazaselenuranesmentioning

confidence: 99%

Substituent Effects on the Stability and Antioxidant Activity of Spirodiazaselenuranes

2015

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Spirodiazaselenuranes are structurally interesting compounds and the stability of these compounds depends highly on the nature of the substituents attached to the nitrogen atoms. Aromatic substituents are known to play important roles in stabilizing the Se-N bonds in spiro compounds. In this study, several spirodiazaselenuranes are synthesized by introducing benzylic and aliphatic substituents to understand their effect on the stability of the Se-N bonds and the antioxidant activity. Replacement of phenyl substituent by benzyl/alkyl groups significantly reduces the stability of the spirodiazaselenuranes and slows down the oxidative cyclization process. The selenium centre in the spiro compounds undergoes further oxidation to produce the corresponding selenurane oxides, which are stable at room temperature. Comparison of the glutathione peroxidase (GPx) mimetic activity of the compounds showed that the diaryl selenides having heterocyclic rings are significantly more active due to the facile oxidation of the selenium centre. However, the activity is reduced significantly for compounds having aliphatic substituents. In addition to GPx activity, the compounds also inhibit peroxynitrite-mediated nitration and oxidation reaction of protein and small molecules, respectively. The experimental observations suggest that the antioxidant activity is increased considerably upon substitution of the aromatic group with the benzylic/aliphatic substituents on the nitrogen atoms.

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“…An increase in the concentrations of oxidizing species would destroy cellular redox balance and lead to the oxidation of proteins, DNA, membrane lipids, and thus mitochondrial dysfunction and ultimately cell death [36]. Anti-oxidative enzymes, such as superoxide dismutase, catalase, and GPx, are the three major reactive oxygen species scavengers in cells and hence protect cells against oxidative damage.…”

Section: Discussionmentioning

confidence: 99%

Engineering human seleno-glutaredoxin containing consecutive rare codons as an artificial glutathione peroxidase

et al. 2012

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The active center of human glutaredoxin (hGrx1) shares a common thioredoxin fold and specific affinity for substrate glutathione (GSH) with natural glutathione peroxidase (GPx). hGrx1 was redesigned to introduce the catalytic selenocysteine residue to imitate the function of antioxidant selenoenzyme GPx in vivo. The human hGrx1 scaffold is a good candidate for potential medical application compared with other animal-originated protein scaffolds. Two consecutive rare codons (AGG-AGG) in the open reading frame of hGrx1 mRNA encoding Arg26-Arg27 residues can reduce seleno-hGrx1 expression level significantly in the Cys auxotrophic Escherichia coli strain BL21cysE51. Therefore, we optimized the rare codons, which resulted in a remarkable increase of the expression level in the Cys auxotrophic cells, which may be sufficient for future medical production. The engineered artificial selenoenzyme displays high GPx catalytic activity, rivaling that of some natural GPx proteins. Kinetic analysis of the engineered seleno-hGrx1 showed a typical ping-pong kinetic mechanism; its catalytic properties are similar to those of some naturally occurring GPx proteins. selenium, selenocysteine, rare codon, artificial enzyme, glutathione peroxidase, glutaredoxin Citation:Zhang W, Luo Q, Wang X P, et al. Engineering human seleno-glutaredoxin containing consecutive rare codons as an artificial glutathione peroxidase.

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Evaluation of sulfur, selenium and tellurium catalysts with antioxidant potential

Cited by 75 publications

References 42 publications

The Metallothionein/Thionein System: An Oxidoreductive Metabolic Zinc Link

The Metallothionein/Thionein System: An Oxidoreductive Metabolic Zinc Link

Substituent Effects on the Stability and Antioxidant Activity of Spirodiazaselenuranes

Engineering human seleno-glutaredoxin containing consecutive rare codons as an artificial glutathione peroxidase

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