• Molecules and Cells
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• v.39 no.1
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• pp.1-5
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• 2016

Peroxiredoxins (Prxs) are a very large and highly conserved family of peroxidases that reduce peroxides, with a conserved cysteine residue, designated the "peroxidatic" Cys ($C_P$) serving as the site of oxidation by peroxides (Hall et al., 2011; Rhee et al., 2012). Peroxides oxidize the $C_P$-SH to cysteine sulfenic acid ($C_P$-SOH), which then reacts with another cysteine residue, named the "resolving" Cys ($C_R$) to form a disulfide that is subsequently reduced by an appropriate electron donor to complete a catalytic cycle. This overview summarizes the status of studies on Prxs and relates the following 10 minireviews.

• Food Science of Animal Resources
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• v.40 no.4
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• pp.601-612
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• 2020

The study assessed the stability for fresh beef patties with the inclusion of clove extract (CE) as a natural antioxidant in comparison to butylated hydroxytoluene (BHT) and ascorbic acid (AA) at frozen storage. Four different patties were made dependent on the added antioxidants: control (added no antioxidants), added with 0.02% BHT, 0.05% AA, and 0.1% CE. Inclusion of BHT, AA, and CE resulted in a significant reduction of thiobarbituric acid reactive substances (TBARS) and hue angle (h°) value and increase of redness (CIE a*) and chroma (C*) values (p<0.05). BHT, AA, and CE were observed effectively to retard lipid oxidation and increase color stability. BHT and AA revealed significantly (p<0.05) higher thiol content than the control and CE. However, the reduction percentage for thiol content in CE treated patties was lower than the control and AA-treated patties from first to last time of storage. Moreover, inclusion of AA and CE led to significantly (p<0.05) increased heme iron content when compared to BHT and the control. In conclusion, CE can replace the application of AA and BHT while improving lipid stability, heme iron content, and color stableness of fresh beef patties throughout frozen storage.

• Journal of the Korean Ceramic Society
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• v.42 no.1
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• pp.50-55
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• 2005

New fast proton-conducting organic-inorganic nanocomposite membranes were successfully fabricated using polymer matrix obtained through proper oxidation of thiol ligands in (3-Mercaptopropyl) trimethoxysilane (MPTS) and hydrolysis/condensation reaction of (3-glycidoxypropyl) trimethoxysilane (GPTS). The obtained nanocomposite membranes showed relatively hirh proton-conductivity over $10^{-2}S/cm$ at $ 25^{circ}C$. The proton conductivities of the fabricated composite membranes increased up to $3.6{\times}10^{-1}$ S/cm cm by increasing temperature and relative humidity to $70^{circ}C$ and 100 $100RH\%$. The high proton conductivity of the composites Is due to the proton conducting path through the GPTS-derived 'pseudo-polyethylene oxide 'network in which sulfonic acid ligands work as a proton donor.

• Korean Journal of Optics and Photonics
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• v.14 no.1
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• pp.97-102
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• 2003

Multi-channel images of 11-MUA(11-Mercaptoundecanoic acid) and 11-MUOH(11-Mercaptoundecanol) self-assembled monolayers were obtained by using two-dimensional surface plasmon resonance (SPR) absorption. The patterning process was simplified by exploiting direct photo-oxidation of thiol bonding (photolysis) instead of conventional photolithography. Sharper images were resolved by using a white light source in combination with a narrow bandpass filter in the visible region, minimizing the diffraction patterns on the images. The line profile calibration of the image contrast caused by different resonance conditions at each point on the sensor surface (at a fixed incident angle) enables us to discriminate the monolayer thickness in nanometer scale. Furthermore, there is no signal degradation such as photo bleaching or quenching, which are common in the detection methods based on fluorescence.

• Applied Microscopy
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• v.35 no.4
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• pp.16-23
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• 2005

Peroxiredoxins (Prxs) are a superfamily of thiol-specific antioxidant proteins present in all organism and involved in the hydroperoxide detoxification of the cell. To determine the structural organization of yeast-Prx, electron microscopic analysis was performed. The average images of yeast-Prxs revealed three different structure, i.e. spherical-shaped structure, ring-shaped structure and irregularly-shaped small particles. In order to analyze the conformational change of yeast-Prx by reduction and oxidation, Prxs were subjected to DTT and $H_2O_2$. In presence of DTT, yeast-Prx showed a high tendency to form a decamer. However, they changed into dimeric or spherical structure in the oxidized state. Here we also show ionic interaction between dimeric subunits is primarily responsible for yeast-Prx oligomerization.

• Proceedings of the Korean Vacuum Society Conference
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• 2011.08a
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• pp.208-209
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• 2011

In this work, we developed self-assembled monolayers (SAMs) of alkanethiols on gold that can release amine groups, when an electrical potential was applied to the gold. The strategy was based on the introduction of the electroactive carbamate group, which underwent the two-electron oxidation with simultaneous release of the amine molecules, to alkanethiols. The synthesis of the designed thiol compounds was achieved by coupling isocyanate-containing compound with hydroquinone. The electroactive thiols were mixed with hydroxyl-containing alkanethiol [$HS(CH_2)_{11}OH$] to form mixed monolayers, and cyclic votammetry was used for the characterization of the release. The mixed SAMs showed a first oxidation peak at +540 mV (versus Ag/AgCl reference electrode), demonstrating irreversible conversion from carbamate to hydroqinone with simultaneous release of the amine groups. The second and third cycles showed typical reversible redox reaction of hydroquinone and quione: the oxidation and reduction occurred at +290 mV and -110 mV, respectively. The measurement of ToF-SIMS further indicates that electrochemical-assisted chemical reaction successfully released amine groups. This new SAM-based electrochemistry would be applicable for direct release of biologically active molecules that contain amine groups.

• Asian-Australasian Journal of Animal Sciences
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• v.33 no.5
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• pp.812-824
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• 2020

Objective: The aim of this work was to assess the effect of fermented blueberry (FB; 2%, 4%, and 6%) on the oxidative stability and volatile molecule profiles of emulsion-type sausage stored at 4℃ for 28 days. Methods: The antioxidant activity of FB was determined through radical-scavenging activity against 2, 2-diphenyl-1-picrylhydrazyl (DPPH) and hydroxyl radicals. Four formulations of sausage treatments with different FB levels (0%, 2%, 4%, 6%) were prepared, then peroxide value (POVs), thiobarbituric acid-reactive substances (TBARS) values, protein carbonyls and thiol groups were measured. The aroma profiles of sausages for each treatment was also determined. Results: The half maximal inhibitory concentration indicated that FB had greater scavenging ability than ascorbic acid against DPPH and hydroxyl radicals. Sausages with FB significantly retarded increases in POVs and TBARS, as well as in the content of protein carbonyls during all storage days (p<0.05). Particularly, 4% and 6% FB-treated sausages had better oxidation inhibition effects. However, FB accelerated the reduction in thiol groups (p<0.05). Additionally, FB inhibits the excessive formation of aldehyde compounds; for example, hexanal, which may cause rancid flavors, decreased from 58.25% to 19.41%. FB also created 6 alcohols (i.e., 2-methyl-1-propanol, 3-methyl-1-butanol, and phenylethyl alcohol), 5 ester compounds (i.e., ethyl acetate, ethyl lactate, and ethyl hexanoate) and 3-hydroxy-2-butanone in the sausages that contribute to sausage flavors. The principal component analysis showed that the aroma profiles of sausages with and without FB are easily identified. Conclusion: The addition of FB could significantly reduce the lipid and protein oxidation and improve oxidative stability for storage. Also, adding FB could inhibit rancid flavors and contribute to sausage flavors.

• Journal of Life Science
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• v.20 no.12
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• pp.1777-1783
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• 2010

Plants generate reactive oxygen species (ROS) as a by-product of normal aerobic metabolism or when exposed to a variety of stress conditions, which can cause widespread damage to biological macromolecules. To protect themselves from oxidative stress, plant cells are equipped with a wide range of antioxidant proteins. However, the detailed reaction mechanisms of these are still unknown. Peroxiredoxins (Prxs) are ubiquitous thiol-containing antioxidants that reduce hydrogen peroxide with an N-terminal cysteine. The active-site cysteine of peroxiredoxins is selectively oxidized to cysteine sulfinic acid during catalysis, which leads to inactivation of peroxidase activity. This oxidation was thought to be irreversible. Recently identified small protein sulphiredoxin (Srx1), which is conserved in higher eukaryotes, reduces cysteine.sulphinic acid in yeast peroxiredoxin. Srx1 is highly induced by $H_2O_2$-treatment and the deletion of its gene causes decreased yeast tolerance to $H_2O_2$, which suggest its involvement in the metabolism of oxidants. Moreover, Srx1 is required for heat shock and oxidative stress induced functional, as well as conformational switch of yeast cytosolic peroxiredoxins. This change enhances protein stability and peroxidase activity, indicating that Srx1 plays a crucial role in peroxiredoxin stability and its regulation mechanism. Thus, the understanding of the molecular basis of Srx1 and its regulation is critical for revealing the mechanism of peroxiredoxin action. We postulate here that Srx1 is involved in dealing with oxidative stress via controlling peroxiredoxin recycling in Arabidopsis. This review article thus will be describing the functions of Prxs and Srx in Arabidopsis thaliana. There will be a special focus on the possible role of Srx1 in interacting with and reducing hyperoxidized Cys-sulphenic acid of Prxs.

• Food Science of Animal Resources
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• v.42 no.5
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• pp.816-832
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• 2022

To evaluate the effects of early postmortem vacuum packaging (VP) on meat quality during postmortem chilled storage, hot-boned lamb was vacuum-packaged at 1, 6, 12, 24, and 48 h postmortem and stored around 2℃ until 168 h postmortem, with lamb packaged in plastic wrap as the control (aerobic packaging). Intramuscular pH decline was delayed when lamb was vacuum packaged at 1, 6, and 12 h postmortem (p<0.05). The lamb vacuum-packaged at 1 h postmortem (VP-1h group) had significantly lower shear force values and purge losses accompanied by lower free thiol group values than other treatments during postmortem storage and was also higher in extractable calpain-1 activity by 6 h postmortem (p<0.05). Free thiol group concentrations were significantly higher after VP at 6 and 12 h postmortem (p<0.05). Packaging lamb under vacuum very early postmortem produced the lowest shear force and purge loss, likely by slowing heat loss and muscle temperature decline, implying that lamb quality is improved by VP when applied very early postmortem. This was at the expense of protein oxidation, which was unrelated to other meat quality measurements, most likely because potential contracture during hot boning confounded its impact. Further research is required to understand the implications of the interaction between protein oxidation, VP, and hot boning on the acceptability of lamb.

• BMB Reports
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• v.33 no.6
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• pp.514-518
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• 2000

Two open reading frames of Haemophilus influenzae, HI0572 and HI0751, showing homology to a yeast thioredoxin peroxidase II (TPx II) and an E. coli thiol peroxidase $P_{20}$, respectively, were cloned and expressed in E. coli, and then the proteins were subsequently purified and characterized. HI0751 protein showed the thioredoxin (Trx)-dependent peroxidase activity, whereas HI0572 protein showed glutathione-dependent peroxidase. The HI0572 is the first peroxiredoxin with glutathione peroxidase activity rather than thioredoxin peroxidase. Purified HI0572 and HI0751 proteins protected specifically the inactivation of glutamine synthetase by metal catalyzed oxidation (MCO) systems composed of $Fe^{3+}$, $O_2$ and mercaptans such as dithiothreitol, ${\beta}-mercaptoethanol$ and glutathione (GSH). Unlike the HI0751 protein, the HI0572 protein was more effective in protecting glutamine synthetase from inactivation by the $GSH/Fe^{3+}/O_2$ system. It seems that these unique properties of the HI0572 protein are due to the structure containing a glutaredoxin domain at it's C-terminal in addition to a peroxiredoxin domain.