The multifaceted nature of peroxiredoxins in chemical biology

Villar, Sebastián F.; Ferrer-Sueta, Gerardo; Denicola, Ana

doi:10.1016/j.cbpa.2023.102355

Cited by 11 publications

(7 citation statements)

References 70 publications

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“…In this case, the peroxidatic cysteine (C P ) reacts with H 2 O 2 to form a transient intermediate, i.e ., sulfenic acid (-SOH), which condenses with an accessible thiol to form intermolecular (with a target protein) or intramolecular (with the resolving cysteine C R ) disulfide bonds. The disulfide is then transferred to the target protein via thiol-disulfide exchange ( 39 , 40 , 41 ). Glutathione peroxidases catalyze the reduction of cytosolic H 2 O 2 in the presence of reduced glutathione (GSH), which is subsequently converted into its oxidized state [glutathione disulfide (GSSG)] ( 42 ).…”

Section: Ros Generation Biochemical Properties and Clearancementioning

confidence: 99%

Redox regulation in lifespan determination

Karagianni,

Bazopoulou

2024

Journal of Biological Chemistry

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Section: Ros Generation Biochemical Properties and Clearancementioning

confidence: 99%

Redox regulation in lifespan determination

Karagianni,

Bazopoulou

2024

Journal of Biological Chemistry

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“…Prdx6, as a peroxidase, has substrate specificity, and its substrates include H 2 O 2 , short-chain hydroperoxides, and phospholipid hydroperoxides [20,21]. Prdx6 binds to oxidized lipid substrates (oxidized membrane phospholipids) and reduces the generation of phospholipid hydroperoxides induced by oxidative stress [22,23]. Also, Prdx6 interacts with phospholemman in a glutathione-dependent manner and depalmitoylates phospholemman via reactive thiol [24].…”

Section: Enzyme Activities and Function Of Prdx6mentioning

confidence: 99%

Unveiling the Significance of Peroxiredoxin 6 in Central Nervous System Disorders

Xue,

Huang,

Zhu

et al. 2024

Antioxidants

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Peroxiredoxin 6 (Prdx6), a unique 1-Cys member of the peroxiredoxin family, exhibits peroxidase activity, phospholipase activity, and lysophosphatidylcholine acyltransferase (LPCAT) activity. Prdx6 has been known to be an important enzyme for the maintenance of lipid peroxidation repair, cellular metabolism, inflammatory signaling, and antioxidant damage. Growing research has demonstrated that the altered activity of this enzyme is linked with various pathological processes including central nervous system (CNS) disorders. This review discusses the distinctive structure, enzyme activity, and function of Prdx6 in different CNS disorders, as well as emphasizing the significance of Prdx6 in neurological disorders.

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“…They form a toroid (doughnut-like) structure of five (six) homodimers, which can split from the toroid in an unstable disulfide conformation ( Figure 3 ). The second resolving cysteine, C R , in the second homodimer subunit forms an inter-subunit disulfide bond with C P upon a reaction with H 2 O 2 [ 44 , 45 , 46 , 47 , 48 , 49 , 50 ]. At first, sulfenic acid (R-SOH) is formed via two-electron reversible oxidation.…”

Section: Redox Sources Vs Redox Buffers In Mitochondria and Cytosolmentioning

confidence: 99%

“…At first, sulfenic acid (R-SOH) is formed via two-electron reversible oxidation. In an atypical mt peroxiredoxin, PRDX5, the intra-subunit S-S bridge, is formed, i.e., within the single subunit [ 44 , 45 , 46 , 47 , 48 ]. The PRDX ring is destabilized when disulfide bonds are formed [ 44 , 46 ].…”

Section: Redox Sources Vs Redox Buffers In Mitochondria and Cytosolmentioning

confidence: 99%

“…The PRDX ring is destabilized when disulfide bonds are formed [ 44 , 46 ]. Finally, the cycle is completed by the reduction of the two disulfide bonds of the homodimer, catalyzed either by a couple of thioredoxins (TRXs) plus NADPH-dependent TRX reductase (TRXR), or by glutathione (GSH)/glutaredoxin (GRX) [ 44 , 45 , 46 , 47 , 48 ] ( Figure 3 ).…”

Section: Redox Sources Vs Redox Buffers In Mitochondria and Cytosolmentioning

confidence: 99%

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Pitfalls of Mitochondrial Redox Signaling Research

Ježek

2023

Antioxidants

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Redox signaling from mitochondria (mt) to the cytosol and plasma membrane (PM) has been scarcely reported, such as in the case of hypoxic cell adaptation or (2-oxo-) 2-keto-isocaproate (KIC) β-like-oxidation stimulating insulin secretion in pancreatic β-cells. Mutual redox state influence between mitochondrial major compartments, the matrix and the intracristal space, and the cytosol is therefore derived theoretically in this article to predict possible conditions, when mt-to-cytosol and mt-to-PM signals may occur, as well as conditions in which the cytosolic redox signaling is not overwhelmed by the mitochondrial antioxidant capacity. Possible peroxiredoxin 3 participation in mt-to-cytosol redox signaling is discussed, as well as another specific case, whereby mitochondrial superoxide release is diminished, whereas the matrix MnSOD is activated. As a result, the enhanced conversion to H2O2 allows H2O2 diffusion into the cytosol, where it could be a predominant component of the H2O2 release. In both of these ways, mt-to-cytosol and mt-to-PM signals may be realized. Finally, the use of redox-sensitive probes is discussed, which disturb redox equilibria, and hence add a surplus redox-buffering to the compartment, where they are localized. Specifically, when attempts to quantify net H2O2 fluxes are to be made, this should be taken into account.

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The multifaceted nature of peroxiredoxins in chemical biology

Cited by 11 publications

References 70 publications

Redox regulation in lifespan determination

Redox regulation in lifespan determination

Unveiling the Significance of Peroxiredoxin 6 in Central Nervous System Disorders

Pitfalls of Mitochondrial Redox Signaling Research

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