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Journal articles on the topic 'Hydrogen peroxide'

To see the other types of publications on this topic, follow the link: Hydrogen peroxide.

Author: Grafiati

Published: 4 June 2021

Last updated: 7 July 2024

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1

Gaetani, GF, AM Ferraris, M. Rolfo, R. Mangerini, S. Arena, and HN Kirkman. "Predominant role of catalase in the disposal of hydrogen peroxide within human erythrocytes." Blood 87, no. 4 (February 15, 1996): 1595–99. http://dx.doi.org/10.1182/blood.v87.4.1595.bloodjournal8741595.

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Purified enzymes were mixed to form a cell-free system that simulated the conditions for removal of hydrogen peroxide within human erythrocytes. Human glutathione peroxidase disposed of hydrogen peroxide (H2O2) at a rate that was only 17% of the rate at which human catalase simultaneously removed hydrogen peroxide. The relative rates observed were in agreement with the relative rates predicted from the kinetic constants of the two enzymes. These results confirm two earlier studies on intact erythrocytes, which refuted the notion that glutathione peroxidase is the primary enzyme for removal of hydrogen peroxide within erythrocytes. The present findings differ from the results with intact cells, however, in showing that glutathione peroxidase accounts for even less than 50% of the removal of hydrogen peroxide. A means is proposed for calculating the relative contribution of glutathione peroxidase and catalase in other cells and species. The present results raise the possibility that the major function of glutathione peroxidase may be the disposal of organic peroxides rather than the removal of hydrogen peroxide.

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2

VM, Aroutiounian. "Hydrogen Peroxide Gas Sensors." Physical Science & Biophysics Journal 5, no. 2 (2021): 1–22. http://dx.doi.org/10.23880/psbj-16000194.

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The results of studies of many types of semiconductor H 2 O 2 sensors are discussed in this review of 195 articles about hydrogen peroxide. The properties of electrochemical detectors, sensors based on organic and inorganic materials, graphene, and nano-sensors are analyzed. Optical and fluorescent sensors, detectors made of porous materials, quantum dots, fibers, and spheres are briefly discussed. The results of our studies in the YSU of hydrogen peroxide sensors made from solid solutions of carbon nanotubes with semiconducting metal oxides are also presented in the review. The fundamentals of the manufacture of biomarkers of respiration containing hydrogen peroxide vapors, which make it possible to judge the degree of a person’s illness with various respiratory diseases (asthma, lung cancer, etc.), are discussed.

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3

Reva, I. V., T. T. Yamamoto, A. N. Gulkov, Y. T. Takafudzhi, S. N. Baldaev, K. S. Pikula, M. V. Indyk, et al. "NEUROPROTECTIVE ROLE OF HYDROGEN PEROXIDE." International Journal of Applied and Fundamental Research (Международный журнал прикладных и фундаментальных исследований) 2, no. 12 2018 (2018): 346–52. http://dx.doi.org/10.17513/mjpfi.12537.

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4

Ajima, A., SG Cao, K. Takahashi, A. Matsushima, Y. Saito, and Y. Inada. "An attempt to determine lipid peroxides with polyethylene glycol‐modified hemin." Biotechnology and Applied Biochemistry 9, no. 1 (February 1987): 53–57. http://dx.doi.org/10.1111/j.1470-8744.1987.tb00462.x.

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Hemin, having two carboxyl groups, was coupled with alpha‐(3‐aminopropyl)‐omega‐methoxypoly(oxyethylene) through the acid‐amide bond formed with carbodiimide. The modified hemin catalyzed the peroxidase reaction in 1,1,1‐trichloroethane using benzoyl peroxide or peroxides in unsaturated fatty acids as the hydrogen acceptor and leuco crystal violet as the hydrogen donor. A basic study on quantitative microanalysis of the lipid peroxides was attempted.

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5

Calabria, Donato, Andrea Pace, Elisa Lazzarini, Ilaria Trozzi, Martina Zangheri, Massimo Guardigli, Silvia Pieraccini, Stefano Masiero, and Mara Mirasoli. "Smartphone-Based Chemiluminescence Glucose Biosensor Employing a Peroxidase-Mimicking, Guanosine-Based Self-Assembled Hydrogel." Biosensors 13, no. 6 (June 14, 2023): 650. http://dx.doi.org/10.3390/bios13060650.

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Chemiluminescence is widely used for hydrogen peroxide detection, mainly exploiting the highly sensitive peroxidase-luminol-H2O2 system. Hydrogen peroxide plays an important role in several physiological and pathological processes and is produced by oxidases, thus providing a straightforward way to quantify these enzymes and their substrates. Recently, biomolecular self-assembled materials obtained by guanosine and its derivatives and displaying peroxidase enzyme-like catalytic activity have received great interest for hydrogen peroxide biosensing. These soft materials are highly biocompatible and can incorporate foreign substances while preserving a benign environment for biosensing events. In this work, a self-assembled guanosine-derived hydrogel containing a chemiluminescent reagent (luminol) and a catalytic cofactor (hemin) was used as a H2O2-responsive material displaying peroxidase-like activity. Once loaded with glucose oxidase, the hydrogel provided increased enzyme stability and catalytic activity even in alkaline and oxidizing conditions. By exploiting 3D printing technology, a smartphone-based portable chemiluminescence biosensor for glucose was developed. The biosensor allowed the accurate measurement of glucose in serum, including both hypo- and hyperglycemic samples, with a limit of detection of 120 µmol L−1. This approach could be applied for other oxidases, thus enabling the development of bioassays to quantify biomarkers of clinical interest at the point of care.

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6

Niimura, Youichi, Yoshitaka Nishiyama, Daisuke Saito, Hirokazu Tsuji, Makoto Hidaka, Tatsurou Miyaji, Toshiro Watanabe, and Vincent Massey. "A Hydrogen Peroxide-Forming NADH Oxidase That Functions as an Alkyl Hydroperoxide Reductase in Amphibacillus xylanus." Journal of Bacteriology 182, no. 18 (September 15, 2000): 5046–51. http://dx.doi.org/10.1128/jb.182.18.5046-5051.2000.

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ABSTRACT The Amphibacillus xylanus NADH oxidase, which catalyzes the reduction of oxygen to hydrogen peroxide with β-NADH, can also reduce hydrogen peroxide to water in the presence of free flavin adenine dinucleotide (FAD) or the small disulfide-containingSalmonella enterica AhpC protein. The enzyme has two disulfide bonds, Cys128-Cys131 and Cys337-Cys340, which can act as redox centers in addition to the enzyme-bound FAD (K. Ohnishi, Y. Niimura, M. Hidaka, H. Masaki, H. Suzuki, T. Uozumi, and T. Nishino, J. Biol. Chem. 270:5812–5817, 1995). The NADH-FAD reductase activity was directly dependent on the FAD concentration, with a second-order rate constant of approximately 2.0 × 106 M−1 s−1. Rapid-reaction studies showed that the reduction of free flavin occurred through enzyme-bound FAD, which was reduced by NADH. The peroxidase activity of NADH oxidase in the presence of FAD resulted from reduction of peroxide by free FADH2 reduced via enzyme-bound FAD. This peroxidase activity was markedly decreased in the presence of oxygen, since the free FADH2 is easily oxidized by oxygen, indicating that this enzyme system is unlikely to be functional in aerobic growing cells. The A. xylanus ahpC gene was cloned and overexpressed in Escherichia coli. When the NADH oxidase was coupled with A. xylanus AhpC, the peroxidase activity was not inhibited by oxygen. The V max values for hydrogen peroxide and cumene hydroperoxide reduction were both approximately 150 s−1. The Km values for hydrogen peroxide and cumene hydroperoxide were too low to allow accurate determination of their values. Both AhpC and NADH oxidase were induced under aerobic conditions, a clear indication that these proteins are involved in the removal of peroxides under aerobic growing conditions.

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7

Féliz-Matos, Leandro, Ninoska Abreu-Placeres, Luis Miguel Hernandez, Carlos Ruiz-Matuk, and Patricia Grau-Grullón. "Evaluation of In-office Vital Tooth Whitening Combined with Different Concentrations of At-home Peroxides: A Randomized Double-blind Clinical Trial." Open Dentistry Journal 13, no. 1 (November 15, 2019): 377–82. http://dx.doi.org/10.2174/1874210601913010377.

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Background: The clinical evidence relate the effect of associating the in-office and at home vital tooth whitening, describing positive effects on tooth color change and reduction of dental sensitivity. Objective: The purpose of this randomized double-blind clinical trial was to evaluate the effect on the shortened application of in-office vital tooth whitening combined with different concentrations of at-home peroxides in the final tooth color change and dental sensitivity. Methods: Randomized double-blind clinical trial with 120 participants between 18-65 years, allocated in four tooth whitening treatment groups: G1= Carbamide Peroxide 10% + Hydrogen Peroxide 40%, G2= Carbamide Peroxide 15% + Hydrogen Peroxide 40%, G3= Carbamide Peroxide 20% + Hydrogen Peroxide 40%, G4= Hydrogen Peroxide 10% + Hydrogen Peroxide 40% was conducted. Tooth color was measured at baseline and dental sensitivity and tooth color change during and after treatment. Results: No statistical significant differences were found in tooth color change (superior arch p= 0.183 / inferior arch p= 0.374), and in dental sensitivity (p=0.268). Conclusion: Reducing the application time of in-office whitening, combined with in-home products was effective in improving the color. All groups resulted in identical final color change and dental sensitivity. Clinicaltrials.gov: NCT02682329 Available from: https://clinicaltrials.gov/ct2/show/NCT02682329?term=hydrogen+peroxide.

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8

Meizler, A., F. A. Roddick, and N. A. Porter. "Continuous enzymatic treatment of 4-bromophenol initiated by UV irradiation." Water Science and Technology 62, no. 9 (November 1, 2010): 2016–20. http://dx.doi.org/10.2166/wst.2010.550.

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Horseradish peroxidase (HRP) can be used for the treatment of halogenated phenolic substances. In the presence of hydrogen peroxide phenols are oxidized to form polymers which undergo partial dehalogenation. However, when immobilized, the peroxidase is subject to inactivation due to blockage of the active sites by the growing polymers and to deactivation by elevated levels of hydrogen peroxide. When HRP immobilized on a novel glass-based support incorporating titanium dioxide is subjected to UV irradiation, hydrogen peroxide is produced and the nascent polymer is removed. In this work a reactor was constructed that utilized HRP immobilized on the novel support and the in situ production of hydrogen peroxide to treat 4-bromophenol as a model substrate. The system was operated for almost 17 hours with no apparent decline in activity.

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9

Cooper, William J., and Richard G. Zepp. "Hydrogen Peroxide Decay in Waters with Suspended Soils: Evidence for Biologically Mediated Processes." Canadian Journal of Fisheries and Aquatic Sciences 47, no. 5 (May 1, 1990): 888–93. http://dx.doi.org/10.1139/f90-102.

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Hydrogen peroxide decay studies have been conducted in suspensions of several well-characterized soils and in natural water samples. Kinetic and product studies indicated that the decay was biologically-mediated, and could be described by pseudo first-order rate expressions. At an initial H2O2 concentration of 0.5 μM, the hydrogen peroxide half-life varied from 1 to 8 h. The decay was inhibited by thermal and chemical sterilization of the soils. Peroxidase activity was inferred in several natural water samples, where the suspended particles catalyzed the oxidation of p-anisidine by hydrogen peroxide. The mass spectrum of the major reaction product indicated that it was the dimer, possibly benzoquinone-4-methoxyanil, a product that also was observed from the horseradish peroxidase-catalyzed oxidation of p-anisidine by hydrogen peroxide.

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10

Gutowicz, Marzena. "Antioxidant and detoxycative mechanisms in central nervous system." Postępy Higieny i Medycyny Doświadczalnej 74 (February 19, 2020): 1–11. http://dx.doi.org/10.5604/01.3001.0013.8548.

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Since the brain contains a large amount of polyunsaturated fatty acids, consumes up to 20% of oxygen used by the whole body and exhibits low antioxidants activity, it seems to be especially vulnerable to oxidative stress. The most important antioxidant enzymes are superoxide dismutase (SOD), which catalyze the dismutation of superoxide anion to hydrogen peroxide, catalase (CAT), which converts toxic hydrogen peroxide to water and oxygen, and glutathione peroxidase (Se-GSHPx), which reduces hydrogen peroxide and organic peroxides with glutathione as the cofactor. Among other detoxifying enzymes, the most significant is glutathione transferase (GST), which shows detoksyvarious catalytic activities allowing for removal of xenobiotics, reducing organic peroxides and oxidized cell components. One of the most important brain nonenzymatic antioxidants is reduced glutathione (GSH), which (individually or in cooperation with peroxidases) participates in the reduction of free radicals, repair of oxidative damage and the regeneration of other antioxidants, such as ascorbate or tocopherol. Glutathione as a cosubstrate of glutathione transferase scavenges toxic electrophilic compounds. Although the etiology of the major neurodegenerative diseases are unknown, numerous data suggest that reactive oxygen species play an important role. Even a small change in the level of antioxidants can leads to the many disorders in the CNS.

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11

Sekaringgalih, Ratri, and Alif Nur Laili Rachmah. "TREATMENT OF THE GELATIN WASTEWATER WITH OZONE PEROXIDE ADVANCED OXIDATION PROCESS." Menara: Jurnal Teknik Sipil 18, no. 2 (July 6, 2023): 130–37. http://dx.doi.org/10.21009/jmenara.v18i2.35143.

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This research aims to decrease the level of COD, BOD5, and color in the liquid waste of the gelatin industry by using the ozonation process and hydrogen peroxide in order to meet the quality standards of the seaweed industrial waste. The reaction between ozone and peroxide called the peroxone process is one of the Advanced Oxidation Processes (AOPs). The combination of ozone with peroxide can result in a cheaper process. The result shows the lowest COD at the time of ozonation 160 minutes with the addition of hydrogen peroxide 30 ml was 932.39 mg/L (37.03%), the lowest BOD5 at ozonation 160 minutes with the addition of 25 ml hydrogen peroxide was 164.32 mg/L (48%) and the lowest color at 80 minutes of ozonation with the addition of 10 ml of hydrogen peroxide is 158 (73.75%). In the AOPs, the decrease in COD and BOD5 was higher than that of ozonation without hydrogen peroxide..

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12

&NA;. "Hydrogen peroxide." Reactions Weekly &NA;, no. 1377 (November 2011): 21. http://dx.doi.org/10.2165/00128415-201113770-00068.

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13

&NA;. "Hydrogen peroxide." Reactions Weekly &NA;, no. 1380 (December 2011): 22–23. http://dx.doi.org/10.2165/00128415-201113800-00079.

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14

&NA;. "Hydrogen peroxide." Reactions Weekly &NA;, no. 1385 (January 2012): 22. http://dx.doi.org/10.2165/00128415-201213850-00076.

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&NA;. "Hydrogen peroxide." Reactions Weekly &NA;, no. 1393 (March 2012): 23. http://dx.doi.org/10.2165/00128415-201213930-00078.

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16

&NA;. "Hydrogen peroxide." Reactions Weekly &NA;, no. 1180 (December 2007): 19. http://dx.doi.org/10.2165/00128415-200711800-00053.

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17

&NA;. "Hydrogen peroxide." Reactions Weekly &NA;, no. 1183 (January 2008): 17. http://dx.doi.org/10.2165/00128415-200811830-00053.

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18

&NA;. "Hydrogen peroxide." Reactions Weekly &NA;, no. 1189 (February 2008): 20–21. http://dx.doi.org/10.2165/00128415-200811890-00061.

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19

&NA;. "Hydrogen peroxide." Reactions Weekly &NA;, no. 1134 (January 2007): 15–16. http://dx.doi.org/10.2165/00128415-200711340-00052.

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20

&NA;. "Hydrogen peroxide." Reactions Weekly &NA;, no. 1140 (February 2007): 12. http://dx.doi.org/10.2165/00128415-200711400-00041.

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21

&NA;. "Hydrogen peroxide." Reactions Weekly &NA;, no. 1365 (August 2011): 24. http://dx.doi.org/10.2165/00128415-201113650-00086.

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22

&NA;. "Hydrogen peroxide." Reactions Weekly &NA;, no. 1368 (September 2011): 21. http://dx.doi.org/10.2165/00128415-201113680-00074.

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&NA;. "Hydrogen peroxide." Reactions Weekly &NA;, no. 1369 (September 2011): 23. http://dx.doi.org/10.2165/00128415-201113690-00082.

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24

&NA;. "Hydrogen peroxide." Reactions Weekly &NA;, no. 474 (October 1993): 6. http://dx.doi.org/10.2165/00128415-199304740-00027.

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25

&NA;. "Hydrogen peroxide." Reactions Weekly &NA;, no. 647 (April 1997): 9. http://dx.doi.org/10.2165/00128415-199706470-00024.

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26

&NA;. "Hydrogen peroxide." Reactions Weekly &NA;, no. 1407 (June 2012): 26. http://dx.doi.org/10.2165/00128415-201214070-00091.

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27

&NA;. "Hydrogen peroxide." Reactions Weekly &NA;, no. 1407 (June 2012): 27. http://dx.doi.org/10.2165/00128415-201214070-00096.

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28

&NA;. "Hydrogen peroxide." Reactions Weekly &NA;, no. 1093 (March 2006): 18. http://dx.doi.org/10.2165/00128415-200610930-00061.

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29

&NA;. "Hydrogen peroxide." Reactions Weekly &NA;, no. 1118 (September 2006): 12–13. http://dx.doi.org/10.2165/00128415-200611180-00036.

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30

&NA;. "Hydrogen peroxide." Reactions Weekly &NA;, no. 1280 (November 2009): 26. http://dx.doi.org/10.2165/00128415-200912800-00085.

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31

&NA;. "Hydrogen peroxide." Reactions Weekly &NA;, no. 1228 (November 2008): 21. http://dx.doi.org/10.2165/00128415-200812280-00057.

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32

&NA;. "Hydrogen peroxide." Reactions Weekly &NA;, no. 1325 (October 2010): 18–19. http://dx.doi.org/10.2165/00128415-201013250-00061.

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33

&NA;. "Hydrogen peroxide." Reactions Weekly &NA;, no. 1304 (June 2010): 20. http://dx.doi.org/10.2165/00128415-201013040-00065.

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34

&NA;. "Hydrogen peroxide." Reactions Weekly &NA;, no. 1307 (June 2010): 27. http://dx.doi.org/10.2165/00128415-201013070-00085.

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35

&NA;. "Hydrogen peroxide." Reactions Weekly &NA;, no. 1016 (August 2004): 10. http://dx.doi.org/10.2165/00128415-200410160-00033.

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36

&NA;. "Hydrogen peroxide." Reactions Weekly &NA;, no. 1041 (March 2005): 12–13. http://dx.doi.org/10.2165/00128415-200510410-00034.

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37

&NA;. "Hydrogen peroxide." Reactions Weekly &NA;, no. 1339 (February 2011): 23. http://dx.doi.org/10.2165/00128415-201113390-00068.

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38

&NA;. "Hydrogen peroxide." Reactions Weekly &NA;, no. 1351 (May 2011): 24. http://dx.doi.org/10.2165/00128415-201113510-00080.

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39

Cina, Stephen J., James C. U. Downs, and Sandra E. Conradi. "Hydrogen Peroxide." American Journal of Forensic Medicine and Pathology 15, no. 1 (March 1994): 44–50. http://dx.doi.org/10.1097/00000433-199403000-00011.

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40

Faraci, Frank M. "Hydrogen Peroxide." Arteriosclerosis, Thrombosis, and Vascular Biology 26, no. 9 (September 2006): 1931–33. http://dx.doi.org/10.1161/01.atv.0000238355.56172.b3.

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41

Saitoh, Shu-ichi, Cuihua Zhang, Johnathan D. Tune, Barry Potter, Takahiko Kiyooka, Paul A. Rogers, Jarrod D. Knudson, Gregory M. Dick, Albert Swafford, and William M. Chilian. "Hydrogen Peroxide." Arteriosclerosis, Thrombosis, and Vascular Biology 26, no. 12 (December 2006): 2614–21. http://dx.doi.org/10.1161/01.atv.0000249408.55796.da.

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42

"Peroxidase activity of hemoglobin and heme destruction in the presence of hydrogen peroxide and CT-DNA." Glasnik hemicara i tehnologa Bosne i Hercegovine, no. 55 (December 29, 2020). http://dx.doi.org/10.35666/ghtbh.2020.55.04.

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The aim of this study was to investigate the peroxidase activity of Hb with different concentrations of hydrogen peroxide and compare it with hypochlorous acid effect on Hb. Hypochlorous acid at higher concentrations decomposed Hb and heme, releasing fee iron ion from the metal center. High concentrations of hydrogen peroxide switched the peroxidase activity of Hb towards the partial Hb and heme destruction. Heme alone was degraded showing that the Hb conformation and protein environment protects Hb from the distraction in the presence of highly increased hydrogen peroxide concentration that occurs as a result of oxidative stress. In the presence of CT-DNA acted inhibition of the peroxidase activity of Hb was observed signaling inhibited hydrogen peroxide consumption.

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43

"Semiconductor gas sensors detecting hydrogen peroxide." Advances in Nanoscience and Nanotechnology 5, no. 1 (October 26, 2021). http://dx.doi.org/10.33140/ann.05.01.04.

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The results of studies of many types of semiconductor H2 O2 sensors are discussed in this review of 185 articles about hydrogen peroxide. The properties of electrochemical detectors, sensors based on organic and inorganic materials, graphene, and nano-sensors are analyzed. Optical and fluorescent sensors, detectors made of porous materials, quantum dots, fibers, and spheres are briefly discussed. The results of our studies in the YSU of hydrogen peroxide sensors made from solid solutions of carbon nanotubes with semiconducting metal oxides are also presented in the review. The fundamentals of the manufacture of biomarkers of respiration containing hydrogen peroxide vapors, which make it possible to judge the degree of a person's illness with various respiratory diseases (asthma, lung cancer, etc.), are discussed.

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44

Stols, E., and Jacques M. Berner. "Ozone leads to an increase of hydrogen peroxide levels and peroxidase activity in two maize varieties." Suid-Afrikaanse Tydskrif vir Natuurwetenskap en Tegnologie 31, no. 1 (March 6, 2012). http://dx.doi.org/10.4102/satnt.v31i1.300.

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The goal of this study was to determine whether ozone induce hydrogen peroxide concentrations and peroxidase activity in two maize cultivars. Hydrogen peroxide levels as well as peroxidase activity was higher in both the ozone treated cultivars.

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45

"Hydrogen peroxide." Reactions Weekly 1853, no. 1 (May 2021): 227. http://dx.doi.org/10.1007/s40278-021-95093-1.

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"Hydrogen peroxide." Reactions Weekly 1837, no. 1 (January 2021): 315. http://dx.doi.org/10.1007/s40278-021-88914-z.

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"Hydrogen peroxide." Reactions Weekly 1849, no. 1 (April 2021): 220. http://dx.doi.org/10.1007/s40278-021-93604-4.

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"Hydrogen peroxide." Reactions Weekly 1885, no. 1 (December 2021): 243. http://dx.doi.org/10.1007/s40278-021-07002-1.

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"Hydrogen peroxide." Reactions Weekly 1861, no. 1 (June 2021): 153. http://dx.doi.org/10.1007/s40278-021-97953-7.

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"Hydrogen-peroxide." Reactions Weekly 1859, no. 1 (June 2021): 180. http://dx.doi.org/10.1007/s40278-021-97276-6.

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