The basics of thiols and cysteines in redox biology and chemistry

Poole, Leslie B.

doi:10.1016/j.freeradbiomed.2014.11.013

Cited by 804 publications

(722 citation statements)

References 133 publications

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“…Members of the Prx (EC 1.11.1.15) family are ubiquitous peroxidases found in almost all kingdoms [17]. The active center of Prx proteins consists of two Cys residues, and one Cys residue is reactive with H 2 O 2 ; thus, members of the Prx family are termed cysteine-dependent peroxidases to distinguish them from heme peroxidases such as horseradish peroxidase [18]. Prx1 is classified as a '2-Cys' Prx, whose two conserved cysteines are a hallmark of its peroxidase activity.…”

Section: Introductionmentioning

confidence: 99%

Dual role of the active-center cysteine in human peroxiredoxin 1: Peroxidase activity and heme binding

Watanabe

Ishimori

Uchida

2017

Biochemical and Biophysical Research Communications

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HBP23, a 23-kDa heme-binding protein identified in rats, is a member of the peroxiredoxin (Prx) family, the primary peroxidases involved in hydrogen peroxide catabolism. Although HBP23 has a characteristic Cys-Pro heme-binding motif, the significance of heme binding to Prx family proteins remains to be elucidated. Here, we examined the effect of heme binding to human peroxiredoxin-1 (PRX1), which has 97% amino acid identity to HBP23. PRX1 was expressed in Escherichia coli and purified to homogeneity. Spectroscopic titration demonstrated that PRX1 binds heme with a 1:1 stoichiometry and a dissociation constant of 0.17 μM. UV-vis spectra of heme-PRX1 suggested that Cys52 is the axial ligand of ferric heme. PRX1 peroxidase activity was lost upon heme binding, reflecting the fact that Cys52 is not only the heme-binding site but also the active center of peroxidase activity. Interestingly, heme binding to PRX1 caused a decrease in the toxicity and degradation of heme, significantly suppressing H 2 O 2 -dependent heme peroxidase activity and degradation of PRX1-bound heme compared with that of free hemin. By virtue of its cytosolic abundance (~20 μM), PRX1 thus functions as a scavenger of cytosolic hemin (<1 μM). Collectively, our results indicate that PRX1 has a dual role; Cys-dependent peroxidase activity and cytosolic heme scavenger.

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Section: Introductionmentioning

confidence: 99%

Dual role of the active-center cysteine in human peroxiredoxin 1: Peroxidase activity and heme binding

Watanabe

Ishimori

Uchida

2017

Biochemical and Biophysical Research Communications

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“…Among the protein-coding amino acids, cysteine is unique, owing both to its intrinsic nucleophilicity and redox sensitivity (1,2). The nucleophilic thiol group allows cysteine to undergo a broad range of redox modifications, including S-sulfenylation (-SOH), S-sulfinylation (-SO 2 H), S-sulfonylation (-SO 3 H), S-nitrosylation (-SNO), S-sulfhydration (-SSH), and S-glutathionylation (-SSG) ( Fig.…”

mentioning

confidence: 99%

The Expanding Landscape of the Thiol Redox Proteome

Yang

Carroll

Liebler

2016

Molecular & Cellular Proteomics

182

111

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Cysteine occupies a unique place in protein chemistry. The nucleophilic thiol group allows cysteine to undergo a broad range of redox modifications beyond classical thiol-disulfide redox equilibria, including S-sulfenylation (-SOH), S-sulfinylation (-SO 2 H), S-sulfonylation (-SO 3 H), S-nitrosylation (-SNO), S-sulfhydration (-SSH), S-glutathionylation (-SSG), and others. Emerging evidence suggests that these post-translational modifications (PTM) are important in cellular redox regulation and protection against oxidative damage. Identification of protein targets of thiol redox modifications is crucial to understanding their roles in biology and disease. However, analysis of these highly labile and dynamic modifications poses challenges. Recent advances in the design of probes for thiol redox forms, together with innovative mass spectrometry based chemoproteomics methods make it possible to perform global, site-specific, and quantitative analyses of thiol redox modifications in complex proteomes.

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“…Cysteine content was diminished after 2-fold exposure. Reduced cysteine content may reflect the changes in reducing potential because cysteine is used as a precursor in the synthesis of glutathione, which reactive compounds like formalin and H 2 O 2 may deplete (Poole 2015). Cysteine protects against free radical damage caused by paraquat (Shoji et al 1992), although the significance of cysteine in ascidians is not known.…”

Section: Amino Acidsmentioning

confidence: 99%

Biochemical changes and drug residues in ascidian Halocynthia roretzi after formalin–hydrogen peroxide treatment regimen designed against soft tunic syndrome

et al. 2017

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Soft tunic syndrome (STS) is a protozoal disease caused by Azumiobodo hoyamushi in the edible ascidian Halocynthia roretzi. Previous studies have proven that combined formalin-hydrogen peroxide (H 2 O 2 ) bath is effective in reducing STS progress and mortality. To secure target animal safety for field applications, toxicity of the treatment needs to be evaluated. Healthy ascidians were bathed for 1 week, 1 h a day at various bathing concentrations. Bathing with 5-and 10-fold optimum concentration caused 100% mortality of ascidians, whereas mortality by 0.5-to 2.0-fold solutions was not different from that of control. Of the oxidative damage parameters, MDA levels did not change after 0.5-and 1.0-fold bathing. However, free radical scavenging ability and reducing power were significantly decreased even with the lower-than-optimal 0.5-fold concentration. Glycogen content tended to increase with 1-fold bathing without statistical significance. All changes induced by the 2-fold bathing were completely or partially restored to control levels 48 h post-bathing. Free amino acid analysis revealed a concentration-dependent decline in aspartic acid and cysteine levels. In contrast, alanine and valine levels increased after the 2-fold bath treatment. These data indicate that the currently established effective disinfectant regimen against the parasitic pathogen is generally safe, and the biochemical changes observed are transient, lasting approximately 48 h at most. Low levels of formalin and H 2 O 2 were detectable 1 h post-bathing; however, the compounds were completely undetectable after 48 h of bathing. Formalin-H 2 O 2 bathing is effective against STS; however, reasonable care is required in the treatment to avoid unwanted toxicity. Drug residues do not present a concern for consumer safety.

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The basics of thiols and cysteines in redox biology and chemistry

Cited by 804 publications

References 133 publications

Dual role of the active-center cysteine in human peroxiredoxin 1: Peroxidase activity and heme binding

Dual role of the active-center cysteine in human peroxiredoxin 1: Peroxidase activity and heme binding

The Expanding Landscape of the Thiol Redox Proteome

Biochemical changes and drug residues in ascidian Halocynthia roretzi after formalin–hydrogen peroxide treatment regimen designed against soft tunic syndrome

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