Artykuły w czasopismach: „Superoxide”

1

Fridovich, Irwin. "Superoxide and superoxide dismutases". Free Radical Biology and Medicine 15, nr 5 (listopad 1993): 472. http://dx.doi.org/10.1016/0891-5849(93)90188-z.

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2

Fridovich, Irwin. "Superoxide Radical and Superoxide Dismutases". Annual Review of Biochemistry 64, nr 1 (czerwiec 1995): 97–112. http://dx.doi.org/10.1146/annurev.bi.64.070195.000525.

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3

Sheng, Yuewei, Isabel A. Abreu, Diane E. Cabelli, Michael J. Maroney, Anne-Frances Miller, Miguel Teixeira i Joan Selverstone Valentine. "Superoxide Dismutases and Superoxide Reductases". Chemical Reviews 114, nr 7 (kwiecień 2014): 3854–918. http://dx.doi.org/10.1021/cr4005296.

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4

Nishiura, Toshiki, Takehiro Ohta, Takashi Ogura, Jun Nakazawa, Masaya Okamura i Shiro Hikichi. "The Conversion of Superoxide to Hydroperoxide on Cobalt(III) Depends on the Structural and Electronic Properties of Azole-Based Chelating Ligands". Molecules 27, nr 19 (28.09.2022): 6416. http://dx.doi.org/10.3390/molecules27196416.

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Conversion from superoxide (O2‒) to hydroperoxide (OOH‒) on the metal center of oxygenases and oxidases is recognized to be a key step to generating an active species for substrate oxidation. In this study, reactivity of cobalt(III)-superoxido complexes supported by facially-capping tridentate tris(3,5-dimethyl-4-X-pyrazolyl)hydroborate ([HB(pzMe2,X)3]‒; TpMe2,X) and bidentate bis(1-methyl-imidazolyl)methylborate ([B(ImN-Me)2Me(Y)]‒; LY) ligands toward H-atom donating reagent (2-hydroxy-2-azaadamantane; AZADOL) has been explored. The oxygenation of the cobalt(II) precursors give the corresponding cobalt(III)-superoxido complexes, and the following reaction with AZADOL yield the hydroperoxido species as has been characterized by spectroscopy (UV-vis, resonance Raman, EPR). The reaction of the cobalt(III)-superoxido species and a reducing reagent ([CoII(C5H5)2]; cobaltocene) with proton (trifluoroacetic acid; TFA) also yields the corresponding cobalt(III)-hydroperoxido species. Kinetic analyses of the formation rates of the cobalt(III)-hydroperoxido complexes reveal that second-order rate constants depend on the structural and electronic properties of the cobalt-supporting chelating ligands. An electron-withdrawing ligand opposite to the superoxide accelerates the hydrogen atom transfer (HAT) reaction from AZADOL due to an increase in the electrophilicity of the superoxide ligand. Shielding the cobalt center by the alkyl group on the boron center of bis(imidazolyl)borate ligands hinders the approaching of AZADOL to the superoxide, although the steric effect is insignificant.

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5

Campanella, Luigi, Gabriele Favero i Mauro Tomassetti. "Superoxide Dismutase Biosensors for Superoxide Radical Analysis". Analytical Letters 32, nr 13 (styczeń 1999): 2559–81. http://dx.doi.org/10.1080/00032719908542988.

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6

Kuratsuji, Tadatoshi, i Noriaki Shinomiya. "Superoxide and Superoxide Dismutase in Bronchial Asthma". Pediatrics International 29, nr 5 (październik 1987): 680–85. http://dx.doi.org/10.1111/j.1442-200x.1987.tb00360.x.

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7

Abreu, Isabel A., José A. Rodriguez i Diane E. Cabelli. "Theoretical Studies of Manganese and Iron Superoxide Dismutases: Superoxide Binding and Superoxide Oxidation". Journal of Physical Chemistry B 109, nr 51 (grudzień 2005): 24502–9. http://dx.doi.org/10.1021/jp052368u.

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8

Wasselin-Trupin, V., G. Baldacchino i B. Hickel. "Détection des radicaux OH et O2 issus de la radiolyse de l'eau par chimiluminescence résolue en temps". Canadian Journal of Physiology and Pharmacology 79, nr 2 (1.02.2001): 171–75. http://dx.doi.org/10.1139/y00-090.

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A new method for the detection of low concentrations of hydroxyl and superoxide radicals, formed by water radiolysis, is described in this article. The method used is the time resolved chemiluminescence. It has been performed with an electron beam delivered by a Febetron 707 accelerator. This method allows to measure hydroxyl and superoxide radical concentrations in a large range of concentrations, between 105 and 108 M.Key words: chemiluminescence, pulse radiolysis, hydroxyl radical, superoxyde radical.[Traduit par la Rédaction]

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9

Miyasaka, Takehiro, Kosuke Endo, Seiichi Mochizuki i Kiyotaka Sakai. "Superoxide Sensors". Sensor Letters 4, nr 2 (1.06.2006): 144–54. http://dx.doi.org/10.1166/sl.2006.014.

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10

BORMAN, STU. "SURPRISING SUPEROXIDE". Chemical & Engineering News Archive 89, nr 4 (24.01.2011): 11. http://dx.doi.org/10.1021/cen-v089n004.p011.

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11

Fridovich, I. "Superoxide dismutases". Journal of Biological Chemistry 264, nr 14 (maj 1989): 7761–64. http://dx.doi.org/10.1016/s0021-9258(18)83102-7.

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12

Ma, Qi, Huaqiang Fang, Wei Shang, Lei Liu, Zhengshuang Xu, Tao Ye, Xianhua Wang, Ming Zheng, Quan Chen i Heping Cheng. "Superoxide Flashes". Journal of Biological Chemistry 286, nr 31 (9.06.2011): 27573–81. http://dx.doi.org/10.1074/jbc.m111.241794.

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13

James, E. R. "Superoxide dismutase". Parasitology Today 10, nr 12 (styczeń 1994): 481–84. http://dx.doi.org/10.1016/0169-4758(94)90161-9.

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14

Pereira, Alice S., Pedro Tavares, Filipe Folgosa, Rui M. Almeida, Isabel Moura i José J. G. Moura. "Superoxide Reductases". European Journal of Inorganic Chemistry 2007, nr 18 (czerwiec 2007): 2569–81. http://dx.doi.org/10.1002/ejic.200700008.

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15

Beissenhirtz, Moritz K., Frieder W. Scheller, Maria S. Viezzoli i Fred Lisdat. "Engineered Superoxide Dismutase Monomers for Superoxide Biosensor Applications". Analytical Chemistry 78, nr 3 (luty 2006): 928–35. http://dx.doi.org/10.1021/ac051465g.

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16

Rodrigues, João V., Isabel A. Abreu, Diane Cabelli i Miguel Teixeira. "Superoxide Reduction Mechanism ofArchaeoglobus fulgidusOne-Iron Superoxide Reductase†". Biochemistry 45, nr 30 (sierpień 2006): 9266–78. http://dx.doi.org/10.1021/bi052489k.

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17

Silaghi-Dumitrescu, Radu. "Superoxide interaction with nickel and iron superoxide dismutases". Journal of Molecular Graphics and Modelling 28, nr 2 (wrzesień 2009): 156–61. http://dx.doi.org/10.1016/j.jmgm.2009.06.001.

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18

Kocabay, Ozge, Emel Emregul, Sümer Aras i Kaan Cebesoy Emregul. "Carboxymethylcellulose–gelatin–superoxidase dismutase electrode for amperometric superoxide radical sensing". Bioprocess and Biosystems Engineering 35, nr 6 (18.01.2012): 923–30. http://dx.doi.org/10.1007/s00449-011-0677-x.

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19

Raha, Sandeep, Gillian E. McEachern, A. Tomoko Myint i Brian H. Robinson. "Superoxides from mitochondrial complex III: the role of manganese superoxide dismutase". Free Radical Biology and Medicine 29, nr 2 (lipiec 2000): 170–80. http://dx.doi.org/10.1016/s0891-5849(00)00338-5.

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20

Ohsaka, Takeo, Yang Tian, Mieko Shioda, Shinjiro Kasahara i Takeyoshi Okajima. "A superoxide dismutase-modified electrode that detects superoxide ion". Chemical Communications, nr 9 (10.04.2002): 990–91. http://dx.doi.org/10.1039/b201197b.

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21

Zhang, Xing, Zhanglong Huang, Tingting Hou, Jiejia Xu, Yanru Wang, Wei Shang, Tao Ye, Heping Cheng, Feng Gao i Xianhua Wang. "Superoxide constitutes a major signal of mitochondrial superoxide flash". Life Sciences 93, nr 4 (sierpień 2013): 178–86. http://dx.doi.org/10.1016/j.lfs.2013.06.012.

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22

Jay, David, Elizabeth J. Garcı́a, Marı́a del Carmen Avila, Eduardo Muñoz i Roberto Gleason. "Superoxide-Superoxide Oxidoreductase Activity of the Captopril-Copper Complex". Archives of Medical Research 33, nr 2 (marzec 2002): 115–22. http://dx.doi.org/10.1016/s0188-4409(01)00375-7.

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23

Tian, Yang, Lanqun Mao, Takeyoshi Okajima i Takeo Ohsaka. "Superoxide Dismutase-Based Third-Generation Biosensor for Superoxide Anion". Analytical Chemistry 74, nr 10 (maj 2002): 2428–34. http://dx.doi.org/10.1021/ac0157270.

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24

Halliwell, B. "Superoxide and superoxide dismutase in chemistry, biology and medicine". FEBS Letters 216, nr 1 (25.05.1987): 169. http://dx.doi.org/10.1016/0014-5793(87)80783-4.

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25

Lundgren, Camilla A. K., Dan Sjöstrand, Olivier Biner, Matthew Bennett, Axel Rudling, Ann-Louise Johansson, Peter Brzezinski, Jens Carlsson, Christoph von Ballmoos i Martin Högbom. "Scavenging of superoxide by a membrane-bound superoxide oxidase". Nature Chemical Biology 14, nr 8 (18.06.2018): 788–93. http://dx.doi.org/10.1038/s41589-018-0072-x.

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26

Huang, Ting-Ting, Michio Yasunami, Elaine J. Carlson, Anne Marie Gillespie, Andrew G. Reaume, Eric K. Hoffman, Pak H. Chan, Richard W. Scott i Charles J. Epstein. "Superoxide-Mediated Cytotoxicity in Superoxide Dismutase-Deficient Fetal Fibroblasts". Archives of Biochemistry and Biophysics 344, nr 2 (sierpień 1997): 424–32. http://dx.doi.org/10.1006/abbi.1997.0237.

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27

Shen, Jian, i J. Andrew McCammon. "Molecular dynamics simulation of superoxide interacting with superoxide dismutase". Chemical Physics 158, nr 2-3 (grudzień 1991): 191–98. http://dx.doi.org/10.1016/0301-0104(91)87066-5.

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28

Peters, T. J. "Superoxide and superoxide dismutase in chemistry, biology and medicine". Clinica Chimica Acta 163, nr 3 (marzec 1987): 353. http://dx.doi.org/10.1016/0009-8981(87)90255-5.

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29

Ewing, James F., i David R. Janero. "Microplate Superoxide Dismutase Assay Employing a Nonenzymatic Superoxide Generator". Analytical Biochemistry 232, nr 2 (grudzień 1995): 243–48. http://dx.doi.org/10.1006/abio.1995.0014.

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30

Liochev, Stefan I., i Irwin Fridovich. "Copper- and Zinc-containing Superoxide Dismutase Can Act as a Superoxide Reductase and a Superoxide Oxidase". Journal of Biological Chemistry 275, nr 49 (25.09.2000): 38482–85. http://dx.doi.org/10.1074/jbc.m007891200.

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31

Murakami, Kazuma, i Takahiko Shimizu. "Cytoplasmic superoxide radical". Communicative & Integrative Biology 5, nr 3 (maj 2012): 255–58. http://dx.doi.org/10.4161/cib.19548.

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32

YUASA, Makoto, Kenichi OYAIZU i Hidenori MURATA. "Superoxide Dismutase Mimics". Oleoscience 6, nr 6 (2006): 307–17. http://dx.doi.org/10.5650/oleoscience.6.307.

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33

Simovic, Misho O., Martin J. D. Bonham, Fikri M. Abu-Zidan i John A. Windsor. "Manganese Superoxide Dismutase". Pancreas 15, nr 1 (lipiec 1997): 78–82. http://dx.doi.org/10.1097/00006676-199707000-00011.

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34

Shaked, Yeala, i Andrew Rose. "Seas of Superoxide". Science 340, nr 6137 (6.06.2013): 1176–77. http://dx.doi.org/10.1126/science.1240195.

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35

&NA;. "Superoxide dismutase cream". Inpharma Weekly &NA;, nr 796 (lipiec 1991): 6. http://dx.doi.org/10.2165/00128413-199107960-00014.

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36

Cai, Jiyang, i Dean P. Jones. "Superoxide in Apoptosis". Journal of Biological Chemistry 273, nr 19 (8.05.1998): 11401–4. http://dx.doi.org/10.1074/jbc.273.19.11401.

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37

Rosenthal, Rosalind A., Susan R. Doctrow i Wyeth B. Callaway. "Superoxide Dismutase Mimics". Antioxidants & Redox Signaling 14, nr 6 (15.03.2011): 1173. http://dx.doi.org/10.1089/ars.2010.3758.

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38

Turner, Craig P., Ashley M. Toye i Owen T. G. Jones. "Keratinocyte Superoxide Generation". Free Radical Biology and Medicine 24, nr 3 (luty 1998): 401–7. http://dx.doi.org/10.1016/s0891-5849(97)00270-0.

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39

Salvemini, Daniela, Carolina Muscoli, Dennis P. Riley i Salvatore Cuzzocrea. "Superoxide Dismutase Mimetics". Pulmonary Pharmacology & Therapeutics 15, nr 5 (październik 2002): 439–47. http://dx.doi.org/10.1006/pupt.2002.0374.

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40

Nozik-Grayck, Eva, Hagir B. Suliman i Claude A. Piantadosi. "Extracellular superoxide dismutase". International Journal of Biochemistry & Cell Biology 37, nr 12 (grudzień 2005): 2466–71. http://dx.doi.org/10.1016/j.biocel.2005.06.012.

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41

Brand, Martin D., Julie A. Buckingham, Telma C. Esteves, Katherine Green, Adrian J. Lambert, Satomi Miwa, Michael P. Murphy, Julian L. Pakay, Darren A. Talbot i Karim S. Echtay. "Mitochondrial superoxide and aging: uncoupling-protein activity and superoxide production". Biochemical Society Symposia 71 (1.03.2004): 203–13. http://dx.doi.org/10.1042/bss0710203.

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Mitochondria are a major source of superoxide, formed by the one-electron reduction of oxygen during electron transport. Superoxide initiates oxidative damage to phospholipids, proteins and nucleic acids. This damage may be a major cause of degenerative disease and aging. In isolated mitochondria, superoxide production on the matrix side of the membrane is particularly high during reversed electron transport to complex I driven by oxidation of succinate or glycerol 3-phosphate. Reversed electron transport and superoxide production from complex I are very sensitive to proton motive force, and can be strongly decreased by mild uncoupling of oxidative phosphorylation. Both matrix superoxide and the lipid peroxidation product 4-hydroxy-trans-2-nonenal can activate uncoupling through endogenous UCPs (uncoupling proteins). We suggest that superoxide releases iron from aconitase, leading to a cascade of lipid peroxidation and the release of molecules such as hydroxy-nonenal that covalently modify and activate the proton conductance of UCPs and other proteins. A function of the UCPs may be to cause mild uncoupling in response to matrix superoxide and other oxidants, leading to lowered proton motive force and decreased superoxide production. This simple feedback loop would constitute a self-limiting cycle to protect against excessive superoxide production, leading to protection against aging, but at the cost of a small elevation of respiration and basal metabolic rate.

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42

Martínez, Alejandra, Carolina Prolo, Damián Estrada, Natalia Rios, María Noel Alvarez, María Dolores Piñeyro, Carlos Robello, Rafael Radi i Lucía Piacenza. "Cytosolic Fe-superoxide dismutase safeguardsTrypanosoma cruzifrom macrophage-derived superoxide radical". Proceedings of the National Academy of Sciences 116, nr 18 (12.04.2019): 8879–88. http://dx.doi.org/10.1073/pnas.1821487116.

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Trypanosoma cruzi, the causative agent of Chagas disease (CD), contains exclusively Fe-dependent superoxide dismutases (Fe-SODs). DuringT. cruziinvasion to macrophages, superoxide radical (O2•−) is produced at the phagosomal compartment toward the internalized parasite via NOX-2 (gp91-phox) activation. In this work,T. cruzicytosolic Fe-SODB overexpressers (pRIBOTEX–Fe-SODB) exhibited higher resistance to macrophage-dependent killing and enhanced intracellular proliferation compared with wild-type (WT) parasites. The higher infectivity of Fe-SODB overexpressers compared with WT parasites was lost in gp91-phox−/−macrophages, underscoring the role of O2•−in parasite killing. Herein, we studied the entrance of O2•−and its protonated form, perhydroxyl radical [(HO2•); pKa= 4.8], toT. cruziat the phagosome compartment. At the acidic pH values of the phagosome lumen (pH 5.3 ± 0.1), high steady-state concentrations of O2•−and HO2•were estimated (∼28 and 8 µM, respectively). Phagosomal acidification was crucial for O2•−permeation, because inhibition of the macrophage H+-ATPase proton pump significantly decreased O2•−detection in the internalized parasite. Importantly, O2•−detection, aconitase inactivation, and peroxynitrite generation were lower in Fe-SODB than in WT parasites exposed to external fluxes of O2•−or during macrophage infections. Other mechanisms of O2•−entrance participate at neutral pH values, because the anion channel inhibitor 5-nitro-2-(3-phenylpropylamino) benzoic acid decreased O2•−detection. Finally, parasitemia and tissue parasite burden in mice were higher in Fe-SODB–overexpressing parasites, supporting the role of the cytosolic O2•−-catabolizing enzyme as a virulence factor for CD.

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43

Nakazawa, H., K. Ichimori, Y. Shinozaki, H. Okino i S. Hori. "Is superoxide demonstration by electron-spin resonance spectroscopy really superoxide?" American Journal of Physiology-Heart and Circulatory Physiology 255, nr 1 (1.07.1988): H213—H215. http://dx.doi.org/10.1152/ajpheart.1988.255.1.h213.

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A recent study has indicated that the generation of an oxygen radical in freeze-clamped myocardium on reperfusion can be directly demonstrated using electron-spin resonance spectroscopy (ESR). However, the results need to be analyzed with caution, since artifactual radicals are misleading problems common to this method. To test whether that reported superoxide is truly the biologically existing radical or an artifactual radical, we performed experiments using isolated, perfused rat and rabbit hearts and open-chest canine hearts subjected to ischemia/reperfusion. Radicals were freeze trapped at 77 degrees K, and ESR measurements were made. The ESR spectra exhibited four free radicals. Among these, two radicals which had been previously claimed as superoxide and a nitrogen-centered radical were shown as mechanically yielded artifactual radicals. These were produced by pulverization of the frozen sample. In artifact-free samples, superoxide could not be detected. The radicals native to the myocardium were identified as coenzyme Q10-. and another radical the species of which remains unclear.

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44

Marklund, Stefan L. "Ceruloplasmin, extracellular-superoxide dismutase, and scavenging of superoxide anion radicals". Journal of Free Radicals in Biology & Medicine 2, nr 4 (styczeń 1986): 255–60. http://dx.doi.org/10.1016/s0748-5514(86)80007-1.

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45

Soteras, Fernando, Ana Algerich, Maite Sanchez, Elena Piazuelo, Jimenez Pilar, Francisco Esteva, Angel Ferrandez i Angel Lanas. "Superoxide anion and superoxide dismutase in human gastroesophageal reflux diseases". Gastroenterology 118, nr 4 (kwiecień 2000): A225. http://dx.doi.org/10.1016/s0016-5085(00)82973-x.

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46

Fridovich, Irwin. "Superoxide Anion Radical (O·̄2), Superoxide Dismutases, and Related Matters". Journal of Biological Chemistry 272, nr 30 (25.07.1997): 18515–17. http://dx.doi.org/10.1074/jbc.272.30.18515.

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Endo, Kosuke, Takehiro Miyasaka, Seiichi Mochizuki, Satoka Aoyagi, Naoyuki Himi, Hiroko Asahara, Katsuhiko Tsujioka i Kiyotaka Sakai. "Development of a superoxide sensor by immobilization of superoxide dismutase". Sensors and Actuators B: Chemical 83, nr 1-3 (marzec 2002): 30–34. http://dx.doi.org/10.1016/s0925-4005(01)01024-3.

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48

Emerit, I., F. Garban, J. Vassy, A. Levy, P. Filipe i J. Freitas. "Superoxide-mediated clastogenesis and anticlastogenic effects of exogenous superoxide dismutase". Proceedings of the National Academy of Sciences 93, nr 23 (12.11.1996): 12799–804. http://dx.doi.org/10.1073/pnas.93.23.12799.

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Skalerič, Uroš, Carl M. Manthey, Stephan E. Mergenhagen, Boris Gašpirc i Sharon M. Wahl. "Superoxide release and superoxide dismutase expression by human gingival fibroblasts". European Journal of Oral Sciences 108, nr 2 (kwiecień 2000): 130–35. http://dx.doi.org/10.1034/j.1600-0722.2000.90771.x.

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Brines, Lisa M., i Julie A. Kovacs. "Understanding the Mechanism of Superoxide Reductase Promoted Reduction of Superoxide". European Journal of Inorganic Chemistry 2007, nr 1 (styczeń 2007): 29–38. http://dx.doi.org/10.1002/ejic.200600461.

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