ArticleThe Journal of biological chemistry2013
The impact of nitric oxide toxicity on the evolution of the glutathione transferase superfamily: a proposal for an evolutionary driving force.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 34 citations in OpenAlex.
- Trial
- Glutathione transferase P1 is modified by palmitate.PloS one · 2024Article
- The Glutathione System: A Journey from Cyanobacteria to Higher Eukaryotes.Antioxidants (Basel, Switzerland) · 2023Review
- A Key Role in Catalysis and Enzyme Thermostability of a Conserved Helix H5 Motif of Human Glutathione Transferase A1-1.International journal of molecular sciences · 2023Article
- The good Samaritan glutathione-S-transferase P1: An evolving relationship in nitric oxide metabolism mediated by the direct interactions between multiple effector molecules.Redox biology · 2023Review
- Glutathione-Biomolecules · 2022Article
- The Relationship of Glutathione-Molecules (Basel, Switzerland) · 2021Review
- The Interaction of Human Glutathione Transferase GSTA1-1 with Reactive Dyes.Molecules (Basel, Switzerland) · 2021Article
- The Peroxidatic Thiol of Peroxiredoxin 1 is Nitrosated by Nitrosoglutathione but Coordinates to the Dinitrosyl Iron Complex of Glutathione.Antioxidants (Basel, Switzerland) · 2020Article
- Glutathione Transferase P1-1 an Enzyme Useful in Biomedicine and as Biomarker in Clinical Practice and in Environmental Pollution.Nutrients · 2019Review
- Erythrocyte glutathione transferase in kidney transplantation: a probe for kidney detoxification efficiency.Cell death & disease · 2018Article
- Evolution of Negative Cooperativity in Glutathione Transferase Enabled Preservation of Enzyme Function.The Journal of biological chemistry · 2016Article
- Erythrocyte glutathione transferase: a general probe for chemical contaminations in mammals.Cell death discovery · 2016Article
Corrections and comments
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Authors and funding
21 authors at 11 institutions in 6 countries.
Funding
Abstract
Glutathione transferases (GSTs) are protection enzymes capable of conjugating glutathione (GSH) to toxic compounds. During evolution an important catalytic cysteine residue involved in GSH activation was replaced by serine or, more recently, by tyrosine. The utility of these replacements represents an enigma because they yield no improvements in the affinity toward GSH or in its reactivity. Here we show that these changes better protect the cell from nitric oxide (NO) insults. In fact the dinitrosyl·diglutathionyl·iron complex (DNDGIC), which is formed spontaneously when NO enters the cell, is highly toxic when free in solution but completely harmless when bound to GSTs. By examining 42 different GSTs we discovered that only the more recently evolved Tyr-based GSTs display enough affinity for DNDGIC (KD < 10(-9) M) to sequester the complex efficiently. Ser-based GSTs and Cys-based GSTs show affinities 10(2)-10(4) times lower, not sufficient for this purpose. The NO sensitivity of bacteria that express only Cys-based GSTs could be related to the low or null affinity of their GSTs for DNDGIC. GSTs with the highest affinity (Tyr-based GSTs) are also over-represented in the perinuclear region of mammalian cells, possibly for nucleus protection. On the basis of these results we propose that GST evolution in higher organisms could be linked to the defense against NO.
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Registered trials
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