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Статті в журналах з теми "Mediated oxidation"

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Автор: Grafiati

Опубліковано: 8 червня 2024

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1

Francioso, Antonio, Alessia Baseggio Conrado, Carla Blarzino, Cesira Foppoli, Elita Montanari, Simone Dinarelli, Alessandra Giorgi, Luciana Mosca та Mario Fontana. "One- and Two-Electron Oxidations of β-Amyloid25-35 by Carbonate Radical Anion (CO3•−) and Peroxymonocarbonate (HCO4−): Role of Sulfur in Radical Reactions and Peptide Aggregation". Molecules 25, № 4 (20 лютого 2020): 961. http://dx.doi.org/10.3390/molecules25040961.

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The β-amyloid (Aβ) peptide plays a key role in the pathogenesis of Alzheimer’s disease. The methionine (Met) residue at position 35 in Aβ C-terminal domain is critical for neurotoxicity, aggregation, and free radical formation initiated by the peptide. The role of Met in modulating toxicological properties of Aβ most likely involves an oxidative event at the sulfur atom. We therefore investigated the one- or two-electron oxidation of the Met residue of Aβ25-35 fragment and the effect of such oxidation on the behavior of the peptide. Bicarbonate promotes two-electron oxidations mediated by hydrogen peroxide after generation of peroxymonocarbonate (HCO4−, PMC). The bicarbonate/carbon dioxide pair stimulates one-electron oxidations mediated by carbonate radical anion (CO3•−). PMC efficiently oxidizes thioether sulfur of the Met residue to sulfoxide. Interestingly, such oxidation hampers the tendency of Aβ to aggregate. Conversely, CO3•− causes the one-electron oxidation of methionine residue to sulfur radical cation (MetS•+). The formation of this transient reactive intermediate during Aβ oxidation may play an important role in the process underlying amyloid neurotoxicity and free radical generation.

2

Nurgaziyeva, E. K., G. S. Tatykhanova, G. A. Mun, V. V. Khutoryanskiy, and S. E. Kudaibergenov. "Oxidation of Cyclohexane Mediated with Gel-Immobilized Gold Nanoparticles." International Journal of Biology and Chemistry 8, no. 1 (2015): 61–66. http://dx.doi.org/10.26577/2218-7979-2015-8-1-61-66.

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3

Clemens, Dahn L., Carol A. Casey, Michael F. Sorrell, and Dean J. Tuma. "Ethanol Oxidation Mediates Impaired Hepatic Receptor-Mediated Enocytosis." Alcoholism: Clinical and Experimental Research 22, no. 4 (June 1998): 778–79. http://dx.doi.org/10.1111/j.1530-0277.1998.tb03866.x.

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4

Rice-Evans, C., and E. Baysal. "Iron-mediated oxidative stress in erythrocytes." Biochemical Journal 244, no. 1 (May 15, 1987): 191–96. http://dx.doi.org/10.1042/bj2440191.

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Erythrocytes subjected extracellularly to iron-mediated oxidant stress undergo haemoglobin oxidation and membrane damage, which can be modulated by maintaining the energy requirements of the cells. The results presented here suggest that a balance exists between the oxidation state of the haemoglobin and the oxidative deterioration of the membrane lipids, which is dependent on the metabolic state of the erythrocytes. These findings have important implications for thalassaemic erythrocytes that may be exposed to excess plasma iron levels, in which excessive membrane-bound iron in the form of haemichromes is a characteristic feature and in which cellular ATP levels are lowered.

5

Faisal, Muhammad, Mukhtiar Ahmed, Sarwat Hussain, Fayaz Ali Larik, and Aamer Saeed. "Investigating the effectiveness of classical and eco-friendly approaches for synthesis of dialdehydes from organic dihalides." Green Processing and Synthesis 8, no. 1 (January 28, 2019): 635–48. http://dx.doi.org/10.1515/gps-2019-0034.

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Abstract Monoaldehydes and dialdehydes are parts of millions of compounds and are extremely versatile intermediates. For the synthesis of monoaldehydes, one impressive approach to date, because of its excellent selectivity, high yield and stability towards over-oxidation and over-reduction, is the oxidation of organic monohalides. Numerous monohalides oxidation based methodologies to afford monoaldehydes are disclosed in literature. In this research work, twelve well-known approaches (well-documented for synthesis of monoaldehydes from monohalides) are investigated for their effectiveness towards synthesis of organic dialdehydes from organic dihalides. The classical approaches under investigation include modified Sommelet oxidation, Kröhnke oxidation, sodium periodate-mediated oxidative protocol, manganese dioxide-based oxidative approach, Kornblum oxidation and Hass-Bender oxidation. The eco-friendly approaches under observation include periodic acid-based IL protocol, periodic acid in vanadium pentoxide-mediated IL method, hydrogen peroxide in vanadium pentoxide-based approach, hydrogen peroxide-mediated IL methodology, IBX-assisted IL protocol and bismuth nitrate-promoted IL technique. In this investigation yield, overoxidation, eco-friendliness, cost-effectiveness and recyclability are the main parameters which are under examination. Hopefully, this research will help chemists in carrying out routine operations in organic synthesis and will also be fruitful to select finest synthetic approach, develop further new transformational methodologies and improve current transformational approaches for the synthesis of dialdehydes.

6

Sequeira, C. A. C., D. M. F. Santos, and P. S. D. Brito. "Mediated and non-mediated electrochemical oxidation of isopropanol." Applied Surface Science 252, no. 17 (June 2006): 6093–96. http://dx.doi.org/10.1016/j.apsusc.2005.11.028.

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7

Miller, D. G., and D. D. M. Wayner. "Electrode-mediated Wacker oxidation of cyclic and internal olefins." Canadian Journal of Chemistry 70, no. 9 (September 1, 1992): 2485–90. http://dx.doi.org/10.1139/v92-314.

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An improved method for the electrode-mediated oxidations of olefins by palladium(II) is described. Current efficiencies from 80% to 95% were obtained in oxidations of 1-decene, styrene, trans-2-octene, and cyclohexene in which perchloric acid was added to a chloride-free solution of a palladium(II) acetate catalyst. The palladium(0) was reoxidized to palladium(II) by reaction with catalytic amounts of benzoquinone, which was, in turn, regenerated by anodic oxidation. Addition of varying amounts of perchloric acid did not affect the current efficiency but accelerated the oxidation reaction, up to a concentration of approximately 0.15 M. The current efficiency remained high (>80%) over the course of the electrode-mediated oxidations of 1-decene, trans-2-octene, and cyclohexene. At the end of the reactions, when the substrate was depleted, a drastic decrease in the current was observed, indicating that the catalytic cycle leading to product was primarily responsible for the electrochemical reaction. It also was shown that the rates of the electrochemical reactions were generally slower than those of homogeneous reactions in which a stoichiometric amount of benzoquinone was used, indicating that the electrochemical regeneration of benzoquinone was mass transport limited at the highest concentrations of perchloric acid. This is in contrast to other reports in the literature that suggested that the homogeneous (non-electrochemical) reactions were actually slower. Reasons for the discrepancy between these results are discussed.

8

Tribble, Diane L., Berbie M. Chu, Gerri A. Levine, Ronald M. Krauss, and Elaine L. Gong. "Selective Resistance of LDL Core Lipids to Iron-Mediated Oxidation." Arteriosclerosis, Thrombosis, and Vascular Biology 16, no. 12 (December 1996): 1580–87. http://dx.doi.org/10.1161/01.atv.16.12.1580.

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Although the nature and consequences of oxidative changes in the chemical constituents of low density lipoproteins (LDLs) have been extensively examined, the physical dynamics of LDL oxidation and the influence of physical organization on the biological effects of oxidized LDLs have remained relatively unexplored. To address these issues, in the present studies we monitored surface- and core-specific peroxidative stress relative to temporal changes in conjugated dienes (CDs), particle charge (an index of oxidative protein modification), and LDL-macrophage interactions. Peroxidative stress in LDL surface and core compartments was evaluated with the site-specific, oxidation-labile fluorescent probes parinaric acid (PnA) and PnA cholesteryl ester (PnCE), respectively. When oxidation was initiated by Cu 2+ , oxidative loss of the core probe (PnCE) closely followed that of the surface probe (PnA), as indicated by the time to 50% probe depletion (t 1/2 ; 15.5±7.8 and 30.4±12 minutes for PnA and PnCE, respectively). Both probes were more resistant in LDL exposed to Fe 3+ (t 1/2 , 53.2±8.1 and 346.7±155.4 minutes), although core probe resistance was much greater with this oxidant (PnCE t 1/2 /PnA t 1/2, 5.8 vs 2.0 for Cu 2+ ). Despite differences in the rate and extent of oxidative changes in Cu 2+ - versus Fe 3+ -exposed LDLs, PnCE loss occurred in close correspondence with CD formation and appeared to precede changes in particle charge under both conditions. Exposure of LDLs to hemin, a lipophilic Fe 3+ -containing porphyrin that becomes incorporated into the LDL particle, resulted in rapid loss of PnCE and simultaneous changes in particle charge, even at concentrations that yielded increases in CDs and thiobarbituric acid–reactive substances similar to those obtained with free Fe 3+ . These results suggest that oxidation of the LDL hydrophobic core occurs in conjunction with accelerated formation of CDs and may be essential for LDL protein modification. In accordance with the known effects of oxidative protein modifications on LDL receptor recognition, exposure of LDLs to Cu 2+ and hemin but not Fe 3+ produced particles that were readily processed by macrophages. Thus, the physical site of oxidative injury appears to be a critical determinant of the chemical and biological properties of LDLs, particularly when oxidized by Fe 3+ .

9

Hu, Jianan, Yun Huang, Minru Xiong, Shafei Luo, Yong Chen, and Yuanjian Li. "The Effects of Natural Flavonoids on Lipoxygenase-Mediated Oxidation of Compounds with a Benzene Ring Structure—A New Possible Mechanism of Flavonoid Anti-Chemical Carcinogenesis and Other Toxicities." International Journal of Toxicology 25, no. 4 (July 2006): 295–301. http://dx.doi.org/10.1080/10915810600746122.

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Numerous studies have strongly suggested that flavonoids exhibit antimutagenic, anticarcinogenic, antiallergic, and anti-inflammatory properties, but the mechanism is still far from clear. In this study, the effect of natural flavonoid compounds, such as green tea polyphenol, epigallocatechin gallate, quercetin, and rutin on lipoxygenase-mediated co-oxidation of guaiacol, benzidine, paraphenylenediamine, and dimethoxybenzidine was investigated. Green tea polyphenol, epigallocatechin gallate, quercetin, and rutin can reduce the co-oxidation reaction speed of tested compounds mediated by soybean lipoxygenase and the production of oxidative products and free radical intermediates. Their median inhibition concentrations on guaiacol oxidation mediated by soybean lipoxygenase were 8.22 mg·L−1, 17.8 μmol·L−1, 41.5 μmol·L−1, and 46.3 μmol·L−1, respectively. These were all significantly lower than glutathione, dithiothreitol, butylated hydroxyanisole and gossypol. The data collected in this study suggest that flavonoids may have an anticarcinogenicity and antitoxicity effect through inhibition of oxidative activation.

10

Luna, Carolina, and Mario Estévez. "Oxidative damage to food and human serum proteins: Radical-mediated oxidation vs. glyco-oxidation." Food Chemistry 267 (November 2018): 111–18. http://dx.doi.org/10.1016/j.foodchem.2017.06.154.

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11

Sang, Shengmin, Chung S. Yang, and Chi-Tang Ho. "Peroxidase-mediated oxidation of catechins." Phytochemistry Reviews 3, no. 1-2 (January 2004): 229–41. http://dx.doi.org/10.1023/b:phyt.0000047794.45076.7c.

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12

Schaefer, Kathryn N., and Jacqueline K. Barton. "DNA-Mediated Oxidation of p53." Biochemistry 53, no. 21 (May 22, 2014): 3467–75. http://dx.doi.org/10.1021/bi5003184.

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13

Shoeb, H. A., B. U. Bowman, A. C. Ottolenghi, and A. J. Merola. "Peroxidase-mediated oxidation of isoniazid." Antimicrobial Agents and Chemotherapy 27, no. 3 (March 1, 1985): 399–403. http://dx.doi.org/10.1128/aac.27.3.399.

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14

Ncanana, Sandile, Lara Baratto, Lucia Roncaglia, Sergio Riva, and Stephanie G. Burton. "Laccase-Mediated Oxidation of Totarol." Advanced Synthesis & Catalysis 349, no. 8-9 (June 4, 2007): 1507–13. http://dx.doi.org/10.1002/adsc.200700005.

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15

Lo, Sheng-Nan, Chien-Chang Shen, Chia-Yu Chang, Keng-Chang Tsai, Chiung-Chiao Huang, Tian-Shung Wu, and Yune-Fang Ueng. "The Effect of Oxidation on Berberine-Mediated CYP1 Inhibition: Oxidation Behavior and Metabolite-Mediated Inhibition." Drug Metabolism and Disposition 43, no. 7 (May 7, 2015): 1100–1107. http://dx.doi.org/10.1124/dmd.115.063966.

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16

Niki, E. "Antioxidants and atherosclerosis." Biochemical Society Transactions 32, no. 1 (February 1, 2004): 156–59. http://dx.doi.org/10.1042/bst0320156.

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The oxidative modification of low-density lipoprotein (LDL) can be induced by various active species by different mechanisms. Vitamin E and other radical-scavenging antioxidants can inhibit the free radical-mediated oxidation of LDL, but they are not effective against LDL oxidation induced by non-radical mechanisms.

17

Biswas, Swapan Kumar, and Titas Biswas. "Metal-free one-pot oxidative conversion: Molecular Iodine Mediated Oxidation Organic Reactions." International Journal of Experimental Research and Review 27 (April 30, 2022): 45–52. http://dx.doi.org/10.52756/ijerr.2022.v27.005.

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Various oxidative compounds such as aldehyde, ketone ester, and acids can be produced in large yields by an effective iodine-mediated oxidative reaction of organic molecules. Molecular iodine is a generally available and commercially extremely inexpensive substance that induces oxidative esterification. With the comparison with different Brønsted acid catalysis, molecular iodine or iodophilic activations proceed the reaction onto a deoxygenation pathway. With only a few mol% of I2, the oxidation occurs very quickly at room temperature. This approach could also be used to transport different benzil derivatives from nonactivated alkynes, such as diaryl acetylenes. Molecular iodine with several mild reagents such as aq. NH3, ∼30% aq. H2O2 and DMSO might be used to convert various one degree alcohols, particularly benzylic alcohols, into the corresponding aromatic amides in suffiently high yields in a one-pot method. Similarly, by treating different benzylic chloride, bromide and iodide with a molecular iodine oxidation medium, the corresponding aromatic amides may be prepared in a one-pot method. The reactions in this section include transformation of several compounds into their respective oxidative products with the metal-free one-pot oxidative.

18

Nandi, Jyoti, John M. Ovian, Christopher B. Kelly, and Nicholas E. Leadbeater. "Oxidative functionalisation of alcohols and aldehydes via the merger of oxoammonium cations and photoredox catalysis." Organic & Biomolecular Chemistry 15, no. 39 (2017): 8295–301. http://dx.doi.org/10.1039/c7ob02243c.

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19

Hirao, Toshikazu. "Selective synthetic methods using vanadium-mediated redox reactions." Pure and Applied Chemistry 77, no. 9 (January 1, 2005): 1539–57. http://dx.doi.org/10.1351/pac200577091539.

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Oxovanadium(V) compounds serve as Lewis acids with oxidation capability and induce one-electron oxidative transformations of organosilicons, organotins, organoaluminums, organoborons, organozincs, and/or their ate complexes. Low-valent vanadium-catalyzed stereoselective reductive transformations, including dehalogenation, pinacol coupling, and the related radical reaction, have been developed by constructing a multicomponent redox system in combination with a coreductant and an additive.

20

Wu, Youxian, Baolin Deng, Huifang Xu, and Hiromi Kornishi. "Chromium(III) Oxidation Coupled with Microbially Mediated Mn(II) Oxidation." Geomicrobiology Journal 22, no. 3-4 (April 2005): 161–70. http://dx.doi.org/10.1080/01490450590945997.

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21

Amente, Stefano, Luigi Lania, Enrico Vittorio Avvedimento, and Barbara Majello. "DNA oxidation drives Myc mediated transcription." Cell Cycle 9, no. 15 (August 2010): 3074–76. http://dx.doi.org/10.4161/cc.9.15.12499.

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22

Athawale, Paresh R., Hanuman P. Kalmode, and D. Srinivasa Reddy. "DBU/O2-Mediated Oxidation of Dienones." Journal of Organic Chemistry 86, no. 13 (June 18, 2021): 9200–9205. http://dx.doi.org/10.1021/acs.joc.1c00529.

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23

Yamamoto, Takahiro, Yasushi Maeda, Seitchi Matsugo, and Hiromi Kitano. "HYDROPEROXYNAPHTHALIMIDE DERIVATIVE-MEDIATED OXIDATION OF LYSOZYME." Photochemistry and Photobiology 62, no. 4 (October 1995): 680–85. http://dx.doi.org/10.1111/j.1751-1097.1995.tb08716.x.

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24

Bulman Page, Philip, Donald Bethell, Paul Stocks, Jag Heer, Andrew Graham, Hooshang Vahedi, Mark Healy, Eric Collington, and David Andrews. "Sulfur Oxidation Mediated by Imine Derivatives." Synlett 12, no. 12 (December 31, 2000): 1355–58. http://dx.doi.org/10.1055/s-1997-1051.

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25

Uyanik, Muhammet, and Kazuaki Ishihara. "Hypervalent iodine-mediated oxidation of alcohols." Chemical Communications, no. 16 (2009): 2086. http://dx.doi.org/10.1039/b823399c.

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26

Bulman Page, Philip C., Jag P. Heer, Donald Bethell, and B. Andrew Lund. "Asymmetric Sulfur Oxidation Mediated by Camphorsulfonylimines." Phosphorus, Sulfur, and Silicon and the Related Elements 153, no. 1 (January 1999): 247–58. http://dx.doi.org/10.1080/10426509908546438.

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27

Baratto, Lara, Andrea Candido, Mattia Marzorati, Francesca Sagui, Sergio Riva, and Bruno Danieli. "Laccase-mediated oxidation of natural glycosides." Journal of Molecular Catalysis B: Enzymatic 39, no. 1-4 (May 2006): 3–8. http://dx.doi.org/10.1016/j.molcatb.2006.01.011.

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28

Navarra, Cristina, Candice Goodwin, Stephanie Burton, Bruno Danieli, and Sergio Riva. "Laccase-mediated oxidation of phenolic derivatives." Journal of Molecular Catalysis B: Enzymatic 65, no. 1-4 (August 2010): 52–57. http://dx.doi.org/10.1016/j.molcatb.2009.12.016.

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29

da Silva Perez, Denilson, Suzelei Montanari, and Michel R. Vignon. "TEMPO-Mediated Oxidation of Cellulose III." Biomacromolecules 4, no. 5 (September 2003): 1417–25. http://dx.doi.org/10.1021/bm034144s.

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30

Zhang, Xueqin, Jun Xia, Jiaoyang Pu, Chen Cai, Gene W. Tyson, Zhiguo Yuan, and Shihu Hu. "Biochar-Mediated Anaerobic Oxidation of Methane." Environmental Science & Technology 53, no. 12 (May 17, 2019): 6660–68. http://dx.doi.org/10.1021/acs.est.9b01345.

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31

KOOY, N., J. ROYALL, H. ISCHIROPOULOS, and J. BECKMAN. "Peroxynitrite-mediated oxidation of dihydrorhodamine 123." Free Radical Biology and Medicine 16, no. 2 (February 1994): 149–56. http://dx.doi.org/10.1016/0891-5849(94)90138-4.

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32

Zeller, Klaus-Peter, Meike Kowallik, and Peter Haiss. "The dimethyldioxirane-mediated oxidation of phenylethyne." Organic & Biomolecular Chemistry 3, no. 12 (2005): 2310. http://dx.doi.org/10.1039/b504296h.

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33

Koritzke, Alanna L., Jacob C. Davis, Rebecca L. Caravan, Matthew G. Christianson, David L. Osborn, Craig A. Taatjes, and Brandon Rotavera. "̇QOOH-mediated reactions in cyclohexene oxidation." Proceedings of the Combustion Institute 37, no. 1 (2019): 323–35. http://dx.doi.org/10.1016/j.proci.2018.05.029.

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34

Rosenfeldt, Erik, Andrew K. Boal, James Springer, Benjamin Stanford, Susan Rivera, Ramesh D. Kashinkunti, and Deborah H. Metz. "Comparison of UV-mediated Advanced Oxidation." Journal - American Water Works Association 105, no. 7 (July 2013): 29–33. http://dx.doi.org/10.1002/j.1551-8833.2013.tb08894.x.

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35

Bolm, Carsten, and Oliver Beckmann. "Zirconium-mediated asymmetric Baeyer-Villiger oxidation." Chirality 12, no. 5-6 (2000): 523–25. http://dx.doi.org/10.1002/(sici)1520-636x(2000)12:5/6<523::aid-chir39>3.0.co;2-z.

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36

Hernandez, Janet, Norma R. Robledo, Luis Velasco, Rodolfo Quintero, Michael A. Pickard, and Rafael Vazquez-Duhalt. "Chloroperoxidase-Mediated Oxidation of Organophosphorus Pesticides." Pesticide Biochemistry and Physiology 61, no. 2 (September 1998): 87–94. http://dx.doi.org/10.1006/pest.1998.2351.

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37

Degendorfer, Georg, Christine Y. Chuang, Hiroaki Kawasaki, Astrid Hammer, Ernst Malle, Fumiyuki Yamakura, and Michael J. Davies. "Peroxynitrite-mediated oxidation of plasma fibronectin." Free Radical Biology and Medicine 97 (August 2016): 602–15. http://dx.doi.org/10.1016/j.freeradbiomed.2016.06.013.

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38

Liu, Meng Ru, and Hai Long Li. "TEMPO-Mediated Oxidation of Unbleached Bagasse Pulp." Advanced Materials Research 496 (March 2012): 71–74. http://dx.doi.org/10.4028/www.scientific.net/amr.496.71.

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Анотація:

In the paper, unbleached bagasse pulp was oxidized with sodium hypochlorite with catalytic amounts of 2,2,6,6-tetramethylpiperidine-1-oxyl radical (TEMPO) and sodium bromide in water. After the TEMPO-mediated oxidation, the oxidized pulp were collected and characterized in terms of morphology, water retention values, crystallinity and deposition properties. The signiﬁcant changes in morphology were observed before and after the oxidation. Crystallinity of cellulose I was nearly unchanged during the oxidation. Water retention value of pulp can be increased from 68.9% to 70.7% by the TEMPO-mediated oxidation. The TEMPO- oxidized pulp was homogeneously dispersed in water when the pulp consistency is 0.1%.

39

Kong, De-Long, Jian-Xun Du, Wei-Ming Chu, Chun-Ying Ma, Jia-Yi Tao, and Wen-Hua Feng. "Ag/Pyridine Co-Mediated Oxidative Arylthiocyanation of Activated Alkenes." Molecules 23, no. 10 (October 22, 2018): 2727. http://dx.doi.org/10.3390/molecules23102727.

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An efficient Ag/pyridine co-mediated oxidative arylthiocyanation of activated alkenes via radical addition/cyclization cascade process was developed. This reaction could be carried out under mild conditions to provide biologically interesting 3-alkylthiocyanato-2-oxindoles in good to excellent yields. Mechanistic studies suggested a unique NCS• radical addition path and clarified the dual roles of catalytic pyridine as base and crucial ligand to accelerate the oxidation of Ag(I) to Ag(II), which is likely oxidant responsible for the formation of NCS• radical. These mechanistic results may impact the design and refinement of other radical based reactions proceeding through catalytic oxidations mediated by Ag(I)-pyridine/persulfate. The chemical versatility of thiocyanate moiety was also highlighted via SCN-tailoring chemistry in post-synthetic transformation for new S-C(sp3/sp2/sp), S-P, and S-S bonds constructions. The protocol provides an easy access to many important bioisosteres in medicinal chemistry and an array of sulfur-containing 2-oxindoles that are difficult to prepare by other approaches.

40

Zhang, Weiran, Ranwei Zhong, Xiangping Qu, Yang Xiang, and Ming Ji. "Effect of 8-Hydroxyguanine DNA Glycosylase 1 on the Function of Immune Cells." Antioxidants 12, no. 6 (June 19, 2023): 1300. http://dx.doi.org/10.3390/antiox12061300.

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Excess reactive oxygen species (ROS) can cause an imbalance between oxidation and anti-oxidation, leading to the occurrence of oxidative stress in the body. The most common product of ROS-induced base damage is 8-hydroxyguanine (8-oxoG). Failure to promptly remove 8-oxoG often causes mutations during DNA replication. 8-oxoG is cleared from cells by the 8-oxoG DNA glycosylase 1 (OGG1)-mediated oxidative damage base excision repair pathway so as to prevent cells from suffering dysfunction due to oxidative stress. Physiological immune homeostasis and, in particular, immune cell function are vulnerable to oxidative stress. Evidence suggests that inflammation, aging, cancer, and other diseases are related to an imbalance in immune homeostasis caused by oxidative stress. However, the role of the OGG1-mediated oxidative damage repair pathway in the activation and maintenance of immune cell function is unknown. This review summarizes the current understanding of the effect of OGG1 on immune cell function.

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Kiffin, Roberta, Christopher Christian, Erwin Knecht, and Ana Maria Cuervo. "Activation of Chaperone-mediated Autophagy during Oxidative Stress." Molecular Biology of the Cell 15, no. 11 (November 2004): 4829–40. http://dx.doi.org/10.1091/mbc.e04-06-0477.

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Oxidatively damaged proteins accumulate with age in almost all cell types and tissues. The activity of chaperone-mediated autophagy (CMA), a selective pathway for the degradation of cytosolic proteins in lysosomes, decreases with age. We have analyzed the possible participation of CMA in the removal of oxidized proteins in rat liver and cultured mouse fibroblasts. Added to the fact that CMA substrates, when oxidized, are more efficiently internalized into lysosomes, we have found a constitutive activation of CMA during oxidative stress. Oxidation-induced activation of CMA correlates with higher levels of several components of the lysosomal translocation complex, but in particular of the lumenal chaperone, required for substrate uptake, and of the lysosomal membrane protein (lamp) type 2a, previously identified as a receptor for this pathway. In contrast with the well characterized mechanism of CMA activation during nutritional stress, which does not require de novo synthesis of the receptor, oxidation-induced activation of CMA is attained through transcriptional up-regulation of lamp2a. We conclude that CMA is activated during oxidative stress and that the higher activity of this pathway under these conditions, along with the higher susceptibility of the oxidized proteins to be taken up by lysosomes, both contribute to the efficient removal of oxidized proteins.

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Jessup, W., V. Darley-Usmar, V. O'Leary, and S. Bedwell. "5-Lipoxygenase is not essential in macrophage-mediated oxidation of low-density lipoprotein." Biochemical Journal 278, no. 1 (August 15, 1991): 163–69. http://dx.doi.org/10.1042/bj2780163.

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The concentration-dependent effects of a series of lipoxygenase inhibitors and antioxidants on the macrophage-mediated oxidative modification of low-density lipoprotein (LDL) were measured. Their influence on macrophage 5-lipoxygenase pathway activity was also studied over the same concentration range. No correlation between inhibition of 5-lipoxygenase and of macrophage-mediated oxidation of LDL was observed. The capacity of the compounds to prevent cell-mediated modification of LDL could be explained in terms of their activity as either aqueous- or lipid-peroxyl radical scavengers. Two potent 5-lipoxygenase inhibitors (MK 886 and Revlon 5901), which had no radical-scavenging properties, were unable to block LDL modification. It is concluded that 5-lipoxygenase is not essential for LDL oxidation by macrophages.

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Sultana, Nazmun, Ulrica Edlund, Chandan Guria, and Gunnar Westman. "Kinetics of Periodate-Mediated Oxidation of Cellulose." Polymers 16, no. 3 (January 30, 2024): 381. http://dx.doi.org/10.3390/polym16030381.

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The oxidation of cellulose to dialdehyde cellulose (DAC) is a process that has received increased interest during recent years. Herein, kinetic modeling of the reaction with sodium periodate as an oxidizing agent was performed to quantify rate-limiting steps and overall kinetics of the cellulose oxidation reaction. Considering a pseudo-first-order reaction, a general rate expression was derived to elucidate the impact of pH, periodate concentration, and temperature on the oxidation of cellulose and concurrent formation of cellulose degradation products. Experimental concentration profiles were utilized to determine the rate constants for the formation of DAC (k1), degradation constant of cellulose (k2), and degradation of DAC (k3), confirming that the oxidation follows a pseudo-first-order reaction. Notably, the increase in temperature has a more pronounced effect on k1 compared to the influence of IO4− concentration. In contrast, k2 and k3 display minimal changes in response to IO4− concentration but increase significantly with increasing temperature. The kinetic model developed may help with understanding the rate-limiting steps and overall kinetics of the cellulose oxidation reaction, providing valuable information for optimizing the process toward a faster reaction with higher yield of the target product.

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Cathcart, M. K., A. K. McNally, D. W. Morel, and G. M. Chisolm. "Superoxide anion participation in human monocyte-mediated oxidation of low-density lipoprotein and conversion of low-density lipoprotein to a cytotoxin." Journal of Immunology 142, no. 6 (March 15, 1989): 1963–69. http://dx.doi.org/10.4049/jimmunol.142.6.1963.

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Abstract Human monocytes, upon activation with opsonized zymosan, altered low-density lipoprotein (LDL) during a 24-h co-incubation, resulting in its oxidation and acquisition of cytotoxic activity against target fibroblast cell lines. Both the oxidation of LDL and its conversion to a cytotoxin were enhanced with time of incubation, with the most substantial changes occurring after 6 h of culture of LDL with activated monocytes. Unactivated monocytes did not mediate either alteration. Superoxide anion (O2-) participated in both the oxidation of LDL and its conversion to a cytotoxin since addition of superoxide dismutase (SOD) at the beginning of the co-incubation inhibited, in a concentration dependent fashion, both the monocyte-mediated oxidation and the monocyte-mediated conversion of LDL to a cytotoxin. As expected, the rate of superoxide anion release was greatest during the respiratory burst, very early in the 24-h incubation (0 to 2 h); however, exposure of LDL to monocytes during the respiratory burst was not required for LDL oxidation. The lower levels of O2- released by the cells hours after the respiratory burst had subsided were sufficient to lead to the initiation of LDL oxidation. Three results indicated that the oxidative modification of LDL into a cytotoxin required O2(-)-independent free radical propagation after O2(-)-dependent initiation. First, oxidation of LDL exposed to the activated, superoxide anion-releasing monocytes for 6 h could be almost completely blocked by the addition at 6 h of the general free radical scavenger butylated hydroxytoluene, but not by SOD. Second, LDL oxidation proceeded even after removal of LDL from the superoxide anion-producing, activated cells after various durations of exposure. Third, the development of substantial levels of lipid peroxidation products and the development of greater cytotoxicity occurred after 6 h of exposure of LDL to activated cells, long after peak O2- release had subsided. These results lead us to conclude that monocyte-mediated oxidation of LDL, leading to its transformation into a cytotoxin, requires release of O2- occurring as a result of activation but not necessarily during the respiratory burst, and also requires O2(-)-independent free radical propagation. The modification of LDL into a potent toxin by activated monocytes may explain the tissue damage in atherosclerotic lesions and other pathologic sites in which inflammatory cells congregate.

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Coelho, Romina, Chiara A. De Benedictis, Ann Katrin Sauer, António J. Figueira, Hélio Faustino, Andreas M. Grabrucker та Cláudio M. Gomes. "Secondary Modification of S100B Influences Anti Amyloid-β Aggregation Activity and Alzheimer’s Disease Pathology". International Journal of Molecular Sciences 25, № 3 (1 лютого 2024): 1787. http://dx.doi.org/10.3390/ijms25031787.

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Proteinaceous aggregates accumulate in neurodegenerative diseases such as Alzheimer’s Disease (AD), inducing cellular defense mechanisms and altering the redox status. S100 pro-inflammatory cytokines, particularly S100B, are activated during AD, but recent findings reveal an unconventional molecular chaperone role for S100B in hindering Aβ aggregation and toxicity. This suggests a potential protective role for S100B at the onset of Aβ proteotoxicity, occurring in a complex biochemical environment prone to oxidative damage. Herein, we report an investigation in which extracellular oxidative conditions are mimicked to test if the susceptibility of S100B to oxidation influences its protective activities. Resorting to mild oxidation of S100B, we observed methionine oxidation as inferred from mass spectrometry, but no cysteine-mediated crosslinking. Structural analysis showed that the folding, structure, and stability of oxidized S100B were not affected, and nor was its quaternary structure. However, studies on Aβ aggregation kinetics indicated that oxidized S100B was more effective in preventing aggregation, potentially linked to the oxidation of Met residues within the S100:Aβ binding cleft that favors interactions. Using a cell culture model to analyze the S100B functions in a highly oxidative milieu, as in AD, we observed that Aβ toxicity is rescued by the co-administration of oxidized S100B to a greater extent than by S100B. Additionally, results suggest a disrupted positive feedback loop involving S100B which is caused by its oxidation, leading to the downstream regulation of IL-17 and IFN-α2 expression as mediated by S100B.

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Zierath, J. R., L. A. Nolte, E. Wahlström, D. Galuska, P. R. Shepherd, B. B. Kahn, and H. Wallberg-Henriksson. "Carrier-mediated fructose uptake significantly contributes to carbohydrate metabolism in human skeletal muscle." Biochemical Journal 311, no. 2 (October 15, 1995): 517–21. http://dx.doi.org/10.1042/bj3110517.

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To determine whether fructose can be utilized as a metabolic substrate for skeletal muscle in man, we investigated its incorporation into glycogen, its oxidation and lactate production in isolated human skeletal muscle. Rates of fructose oxidation and incorporation into glycogen increased in the presence of increasing fructose concentrations (0.1-1.0 mM). Lactate production increased 3-fold when extracellular fructose was increased from 0.1 to 0.5 mM. Cytochalasin B, a competitive inhibitor of hexose transport mediated by the GLUT1 and GLUT4 facilitative glucose transporters, completely inhibited insulin-stimulated glucose incorporation into glycogen and glucose oxidation (P < 0.01), but did not alter fructose incorporation into glycogen or fructose oxidation. Insulin (1000 mu-units/ml) increased glucose incorporation into glycogen 2.7-fold and glucose oxidation 2.3-fold, whereas no effect on fructose incorporation into glycogen or fructose oxidation was noted. A physiological concentration of glucose (5 mM) decreased the rate of 0.5 mM fructose incorporation into glycogen by 60% (P < 0.001), whereas fructose oxidation was not altered in the presence of 5 mM glucose. Irrespective of fructose concentration, the majority of fructose taken up underwent non-oxidative metabolism. Lactate production accounted for approx. 80% of the fructose metabolism in the basal state and approx. 70% in the insulin (1000 mu-units/ml)-stimulated state. In the presence of 5 mM glucose, physiological concentrations of fructose could account for approximately 10-30% of hexose (glucose + fructose) incorporation into glycogen under non-insulin-stimulated conditions. In conclusion, fructose appears to be transported into human skeletal muscle via a carrier-mediated system that does not involve GLUT4 or GLUT1. Furthermore, under physiological conditions, fructose can significantly contribute to carbohydrate metabolism in human skeletal muscle.

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Haunreiter, Kurt J., Anthony B. Dichiara, and Rick Gustafson. "Nanocellulose by Ammonium Persulfate Oxidation: An Alternative to TEMPO-Mediated Oxidation." ACS Sustainable Chemistry & Engineering 10, no. 12 (March 16, 2022): 3882–91. http://dx.doi.org/10.1021/acssuschemeng.1c07814.

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Okita, Yusuke, Tsuguyuki Saito, and Akira Isogai. "Entire Surface Oxidation of Various Cellulose Microfibrils by TEMPO-Mediated Oxidation." Biomacromolecules 11, no. 6 (June 14, 2010): 1696–700. http://dx.doi.org/10.1021/bm100214b.

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49

de Koning, Charles B., Fatema Jagot, Izak Minnie, Aliyaah Rahman, Songeziwe Ntsimango, and Kennedy J. Ngwira. "Hydrogen-Bonded Xanthones as Potential UV Absorbers: The Synthesis of Xanthones from Bio-Renewable Cardanol Utilizing a Ceric Ammonium Sulfate (CAS)-Mediated Oxidation Reaction." SynOpen 06, no. 01 (February 2022): 58–66. http://dx.doi.org/10.1055/s-0040-1719903.

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AbstractThe synthesis of hydrogen-bonded xanthones by using biorenewable hydrogenated cardanol (3-pentadecylphenol) is described. Hydrogenated cardanol was initially converted into various hydroxybenzophenones. These benzophenones were converted into xanthones by utilizing an oxidative ceric ammonium sulfate-mediated reaction. A subsequent ruthenium-mediated late-stage oxidation of the xanthones provided hydrogen-bonded xanthones, which displayed good UVA and UVB absorbing properties.

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Yalamanoglu, Ayla, Jeremy W. Deuel, Ryan C. Hunt, Jin Hyen Baek, Kathryn Hassell, Katie Redinius, David C. Irwin, Dominik J. Schaer, and Paul W. Buehler. "Depletion of haptoglobin and hemopexin promote hemoglobin-mediated lipoprotein oxidation in sickle cell disease." American Journal of Physiology-Lung Cellular and Molecular Physiology 315, no. 5 (November 1, 2018): L765—L774. http://dx.doi.org/10.1152/ajplung.00269.2018.

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Intravascular sickling and lysis of red blood cells, a hallmark feature of sickle cell disease (SCD), releases hemoglobin (Hb) into the circulation. Increased cell-free Hb has been linked to vasculopathy and in vitro lipid oxidation. Scavenger plasma proteins haptoglobin (Hp) and hemopexin (Hpx) can attenuate cell-free Hb and total plasma heme lipid-oxidative capacity but are depleted in SCD. Here, we isolated lipids from BERK-SS mice, guinea pigs (GP) infused with heme-albumin, and patients with SCD undergoing regular exchange transfusion therapy and evaluated the level of lipid oxidation. Malondialdehyde formation, an end product of lipid peroxidation, was increased in BERK-SS mice, purified lipid fractions of the heme-albumin infused GP, and patients with SCD compared with controls. In humans, the extent of lipid oxidation was associated with the absence of Hp as well as decreased Hpx in plasma samples. Postmortem pulmonary tissue obtained from patients with SCD demonstrated oxidized LDL deposition in the pulmonary artery. The relationship between no Hp and low Hpx levels with greater LDL and HDL oxidation demonstrates the loss of protection against cell-free Hb and total plasma heme-mediated lipid oxidation and tissue injury in SCD. Strategies to protect against plasma lipid oxidation by cell-free Hb and total plasma heme (e.g., therapeutic Hp and Hpx replacement) may diminish the deleterious effects of cell-free Hb and total plasma heme toward the vascular system in SCD.