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Journal articles on the topic 'Superoxise dismutase'

Author: Grafiati

Published: 2 June 2025

Last updated: 31 July 2025

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1

Park, Joong-ho, and Jae-heon Kim. "Comparison of enzyme activities of the native and N-terminal 6xHis-tagged Fe supreoxide dismutase from Streptomyces subrutilus P5." Korean Journal of Microbiology 52, no. 2 (2016): 230–35. http://dx.doi.org/10.7845/kjm.2016.6030.

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2

Öhman, Michael, and Stefan L. Marklund. "Plasma extracellular superoxide dismutase and erythrocyte Cu, Zn-containing superoxide dismutase in alcoholics treated with disulfiram." Clinical Science 70, no. 4 (1986): 365–69. http://dx.doi.org/10.1042/cs0700365.

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1. Disulfiram has long been used in the treatment of chronic alcoholism. It is in vivo partially reduced to diethyldithiocarbamate, which is an efficient inhibitor of Cu, Zn-containing superoxide dismutase both in vitro and in vivo. The recently described extracellular superoxide dismutase is even more sensitive to diethyldithiocarbamate than Cu, Zn-superoxide dismutase. 2. To test for the possibility that long term treatment with disulfiram leads to inhibition of the superoxide dismutases, plasma extracellular superoxide dismutase and erythrocyte Cu, Zn-superoxide dismutase were determined in

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3

Schäfer, G., and S. Kardinahl. "Iron superoxide dismutases: structure and function of an archaic enzyme." Biochemical Society Transactions 31, no. 6 (2003): 1330–34. http://dx.doi.org/10.1042/bst0311330.

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Iron and manganese superoxide dismutases are phylogenetically closely related. They are compared by in silico analysis with regard to their metal specificity and their three-dimensional structure. Special attention is given to the structure and properties of superoxide dismutases from archaeal prokaryotes. The mechanism and the extreme thermostability of superoxide dismutase from Sulfolobus acidocaldarius are discussed on the basis of its high-resolution X-ray structure. An alternating-site mechanism and an evolutionary origin of superoxide dismutases under the environmental conditions on the

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4

Gutteridge, J. M. C., and J. V. Bannister. "Copper + zinc and manganese superoxide dismutases inhibit deoxyribose degradation by the superoxide-driven Fenton reaction at two different stages. Implications for the redox states of copper and manganese." Biochemical Journal 234, no. 1 (1986): 225–28. http://dx.doi.org/10.1042/bj2340225.

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When OH. radicals are formed in a superoxide-driven Fenton reaction, in which O2.- is generated enzymically, deoxyribose degradation is effectively inhibited by CuZn- and Mn-superoxide dismutases. The products of this reaction are H2O2 and a Fe3+-EDTA chelate. The mixing of H2O2 and a Fe3+-EDTA chelate also generates OH. radicals able to degrade deoxyribose with the release of thiobarbituric acid-reactive material. This reaction too is inhibited by CuZn- and Mn-superoxide dismutases, suggesting that most of the OH. is formed by a non-enzymic O2.- -dependent reduction of the Fe3+-EDTA chelate.

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5

Meier, B., C. Michel, M. Saran, J. Hüttermann, F. Parak, and G. Rotilio. "Kinetic and spectroscopic studies on a superoxide dismutase from Propionibacterium shermanii that is active with iron or manganese: pH-dependence." Biochemical Journal 310, no. 3 (1995): 945–50. http://dx.doi.org/10.1042/bj3100945.

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Kinetic studies were performed on the superoxide dismutases isolated from the anaerobic bacterium Propionibacterium shermanii as active enzymes with either iron or manganese, which were naturally incorporated into the same molecule depending on the metal supply. Both the Fe- and Mn- forms showed decreasing activity with increasing pH. This suggests the protonation of some groups near the metal, possibly a metal-bound water molecule. Thus the kinetic behaviour of this superoxide dismutase is much more dependent on the protein structure than on the metal incorporated into the active site. The se

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6

Hunaiti, A. "Radial Diffusion as a Simple and Rapid Method for Screening Superoxide Dismutase Activity." Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 24, no. 5 (1987): 511–12. http://dx.doi.org/10.1177/000456328702400515.

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Superoxide dismutases are of great interest due to their increasing medical applications in therapy and diagnosis of some diseases. The radial diffusion assay was evaluated for its usefulness as a simple, cheap and accurate assay for screening superoxide dismutase activity. In this assay O2− radicals were generated from the interaction of reduced riboflavin with molecular oxygen upon exposure of agar gel containing riboflavin and N,N,N̄,N̄-tetramethylethylene diamine (TEMED) to light. If nitrotctrazolium dye is also present, it will be reduced to the blue insoluble formazan, whilst if superoxi

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7

BATTISTONI, Andrea, Silvia FOLCARELLI, Roberta GABBIANELLI, Concetta CAPO, and Giuseppe ROTILIO. "The Cu,Zn superoxide dismutase from Escherichia coli retains monomeric structure at high protein concentration. Evidence for altered subunit interaction in all the bacteriocupreins." Biochemical Journal 320, no. 3 (1996): 713–16. http://dx.doi.org/10.1042/bj3200713.

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Gel-filtration chromatography experiments performed at high protein concentrations demonstrate that the Cu,Zn superoxide dismutase from Escherichia coli is monomeric irrespective of the buffer and of ionic strength. The catalytic activity of the recombinant enzyme is comparable with that of eukaryotic isoenzymes, indicating that the dimeric structure commonly found in Cu,Zn superoxide dismutases is not necessary to ensure efficient catalysis. The analysis of the amino acid sequences suggests that an altered interaction between subunits occurs in all bacterial Cu,Zn superoxide dismutases. The s

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8

Canini, Antonella, Patrizia Albertano, Donatella Leonardi, Daniela Di Somma, and Maria Grilli Caiola. "Superoxide dismutase in cyanobacteria of the Baltic Sea." Algological Studies/Archiv für Hydrobiologie, Supplement Volumes 83 (December 19, 1996): 129–43. http://dx.doi.org/10.1127/algol_stud/83/1996/129.

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9

Battistoni, A. "Role of prokaryotic Cu,Zn superoxide dismutase in pathogenesis." Biochemical Society Transactions 31, no. 6 (2003): 1326–29. http://dx.doi.org/10.1042/bst0311326.

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Several bacterial pathogens possess sodC genes that encode periplasmic or membrane-associated Cu,Zn superoxide dismutases. Since professional phagocytes generate large amounts of reactive oxygen species to control the growth of invading micro-organisms, Cu,Zn superoxide dismutase might protect infectious bacteria from oxy-radical damage and facilitate their survival within the host. This idea has gained support from studies showing that sodC-null mutants of different bacteria are less virulent than their parental wild-type strains, and from the discovery that, despite apparent dispensability f

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10

Chary, P., D. Dillon, A. L. Schroeder, and D. O. Natvig. "Superoxide dismutase (sod-1) null mutants of Neurospora crassa: oxidative stress sensitivity, spontaneous mutation rate and response to mutagens." Genetics 137, no. 3 (1994): 723–30. http://dx.doi.org/10.1093/genetics/137.3.723.

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Abstract Enzymatic superoxide-dismutase activity is believed to be important in defense against the toxic effects of superoxide. Although superoxide dismutases are among the best studied proteins, numerous questions remain concerning the specific biological roles of the various superoxide-dismutase types. In part, this is because the proposed damaging effects of superoxide are manifold, ranging from inactivation of certain metabolic enzymes to DNA damage. Studies with superoxide-deficient mutants have proven valuable, but surprisingly few such studies have been reported. We have constructed an

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11

James, E. R. "Superoxide dismutase." Parasitology Today 10, no. 12 (1994): 481–84. http://dx.doi.org/10.1016/0169-4758(94)90161-9.

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12

Park, Eun-Jeong, Haeng-Soon Lee, Suk-Yoon Kwon, Kwan-Sam Choi, and Sang-Soo Kwak. "Transgenic Tomato Plants That Overexpress Superoxide Dismutase in Fruits." Journal of Plant Biotechnology 29, no. 1 (2002): 7–13. http://dx.doi.org/10.5010/jpb.2002.29.1.007.

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13

Kocabay, Ozge, Emel Emregul, Sümer Aras, and Kaan Cebesoy Emregul. "Carboxymethylcellulose–gelatin–superoxidase dismutase electrode for amperometric superoxide radical sensing." Bioprocess and Biosystems Engineering 35, no. 6 (2012): 923–30. http://dx.doi.org/10.1007/s00449-011-0677-x.

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14

MEIER, Beate, Christoph SCHERK, Marius SCHMIDT, and Fritz PARAK. "pH-dependent inhibition by azide and fluoride of the iron superoxide dismutase from Propionibacterium shermanii." Biochemical Journal 331, no. 2 (1998): 403–7. http://dx.doi.org/10.1042/bj3310403.

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The iron-containing superoxide dismutase from Propionibacterium shermanii shows, in contrast with other iron superoxide dismutases, only a minor inhibition by azide or fluoride (10–100 mM) of up to 23% at pH 7.8. The activity of the protein with Mn bound to the active site was not diminished under the same conditions. The binding constant between azide and the Fe3+ ion was determined as approx. 2 mM and for fluoride approx. 2.3 mM; they are so far comparable to those known for other iron superoxide dismutases. This seems to be a discrepancy because all other iron superoxide dismutases so far k

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15

IÑARREA, Pedro, Hadi MOINI, Daniel RETTORI, et al. "Redox activation of mitochondrial intermembrane space Cu,Zn-superoxide dismutase." Biochemical Journal 387, no. 1 (2005): 203–9. http://dx.doi.org/10.1042/bj20041683.

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The localization of Cu,Zn-superoxide dismutase in the mitochondrial intermembrane space suggests a functional relationship with superoxide anion (O2•−) released into this compartment. The present study was aimed at examining the functionality of Cu,Zn-superoxide dismutase and elucidating the molecular basis for its activation in the intermembrane space. Intact rat liver mitochondria neither scavenged nor dismutated externally generated O2•−, unless the mitochondrial outer membrane was disrupted selectively by digitonin. The activation of the intermembrane space Cu,Zn-superoxide dismutase follo

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16

Kwak, Yeon-Ju, and Jong-Sang Kim. "Changes of Chlorophyll and SOD-like Activities of Chinese Chives Dehydrated at Different Heat Treatments." Journal of the Korean Society of Food Science and Nutrition 38, no. 7 (2009): 879–84. http://dx.doi.org/10.3746/jkfn.2009.38.7.879.

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17

Holovská, K., V. Lenártová, K. Holovská, and P. Javorský. "Characterization of superoxide dismutase in the rumen bacteriumStreptococcus bovis." Veterinární Medicína 47, No. 2 - 3 (2012): 38–44. http://dx.doi.org/10.17221/5801-vetmed.

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Superoxide dismutase (SOD) isoenzymes of the rumen bacterium Streptococcus bovis 4/1 were studied. Native PAGE showed a single band of Mn-SOD, unaffected by 10 mM cyanide or 5 mM hydrogen peroxide under both aerobic and anaerobic growth conditions. When the metals were removed from the growth medium by Chelex 100, the addition of manganese increased enzymatic activity, while addition of iron inhibited SOD activity. Changes in Mn-SOD and glutathione peroxidase (GSHPx) activities evoked by paraquat and increased values of TBARS indicated that these enzymes were not able to sufficiently prevent o

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18

Vinita, Thakur. "Role of Superoxide Dismutase and Glutathione Peroxidase in Infertility." International Journal of Scientific Research 2, no. 11 (2012): 353–54. http://dx.doi.org/10.15373/22778179/nov2013/112.

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19

Seshadri, Gokulakrishnan, Pao Lin Che, Archana V. Boopathy, and Michael E. Davis. "Characterization of Superoxide Dismutases in Cardiac Progenitor Cells Demonstrates a Critical Role for Manganese Superoxide Dismutase." Stem Cells and Development 21, no. 17 (2012): 3136–46. http://dx.doi.org/10.1089/scd.2012.0191.

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20

Raha, Sandeep, Gillian E. McEachern, A. Tomoko Myint, and Brian H. Robinson. "Superoxides from mitochondrial complex III: the role of manganese superoxide dismutase." Free Radical Biology and Medicine 29, no. 2 (2000): 170–80. http://dx.doi.org/10.1016/s0891-5849(00)00338-5.

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21

YUASA, Makoto, Kenichi OYAIZU, and Hidenori MURATA. "Superoxide Dismutase Mimics." Oleoscience 6, no. 6 (2006): 307–17. http://dx.doi.org/10.5650/oleoscience.6.307.

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22

Simovic, Misho O., Martin J. D. Bonham, Fikri M. Abu-Zidan, and John A. Windsor. "Manganese Superoxide Dismutase." Pancreas 15, no. 1 (1997): 78–82. http://dx.doi.org/10.1097/00006676-199707000-00011.

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23

&NA;. "Superoxide dismutase cream." Inpharma Weekly &NA;, no. 796 (1991): 6. http://dx.doi.org/10.2165/00128413-199107960-00014.

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24

Rosenthal, Rosalind A., Susan R. Doctrow, and Wyeth B. Callaway. "Superoxide Dismutase Mimics." Antioxidants & Redox Signaling 14, no. 6 (2011): 1173. http://dx.doi.org/10.1089/ars.2010.3758.

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25

Salvemini, Daniela, Carolina Muscoli, Dennis P. Riley, and Salvatore Cuzzocrea. "Superoxide Dismutase Mimetics." Pulmonary Pharmacology & Therapeutics 15, no. 5 (2002): 439–47. http://dx.doi.org/10.1006/pupt.2002.0374.

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26

Nozik-Grayck, Eva, Hagir B. Suliman, and Claude A. Piantadosi. "Extracellular superoxide dismutase." International Journal of Biochemistry & Cell Biology 37, no. 12 (2005): 2466–71. http://dx.doi.org/10.1016/j.biocel.2005.06.012.

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27

Fridovich, Irwin. "Superoxide and superoxide dismutases." Free Radical Biology and Medicine 15, no. 5 (1993): 472. http://dx.doi.org/10.1016/0891-5849(93)90188-z.

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28

Sanchez-Moreno, M., M. Monteoliva, A. Fatou, and M. A. García-Ruiz. "Superoxide dismutase fromAscaris suum." Parasitology 97, no. 2 (1988): 345–53. http://dx.doi.org/10.1017/s0031182000058546.

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SummaryThree superoxide dismutases (SOD) (EC 1.15.1.1) were detected in homogenates ofAscaris suum. Each of the three forms of SOD was purified by a sequence of multiple differential centrifugations, ammonium sulphate precipitation, ion-exchange chromatography and G-75 Sephadex column chromatography. The three forms of SOD were present in different cellular locations; one in the cytoplasmic fraction, sensitive to cyanide and hydrogen peroxide, and two in the mitochondrial fraction, one of which was cyanide sensitive. The SOD forms presented clear differences in their electrophoretic patterns.

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29

Lancaster, Vanessa L., Russell LoBrutto, Fabiyola M. Selvaraj, and Robert E. Blankenship. "A Cambialistic Superoxide Dismutase in the Thermophilic Photosynthetic Bacterium Chloroflexus aurantiacus." Journal of Bacteriology 186, no. 11 (2004): 3408–14. http://dx.doi.org/10.1128/jb.186.11.3408-3414.2004.

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ABSTRACT Superoxide dismutase from the thermophilic anoxygenic photosynthetic bacterium Chloroflexus aurantiacus was cloned, purified, and characterized. This protein is in the manganese- and iron-containing family of superoxide dismutases and is able to use both manganese and iron catalytically. This appears to be the only soluble superoxide dismutase in C. aurantiacus. Iron and manganese cofactors were identified by using electron paramagnetic resonance spectroscopy and were quantified by atomic absorption spectroscopy. By metal enrichment of growth media and by performing metal fidelity stu

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30

Fridovich, I. "Superoxide dismutases." Journal of Biological Chemistry 264, no. 14 (1989): 7761–64. http://dx.doi.org/10.1016/s0021-9258(18)83102-7.

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31

Park, Jae-seung, and Jae-heon Kim. "Secretion of the iron containing superoxide dismutase of Streptomyces subrutilus P5." Korean Journal of Microbiology 51, no. 2 (2015): 108–14. http://dx.doi.org/10.7845/kjm.2015.5019.

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32

Fridovich, Irwin. "Superoxide Radical and Superoxide Dismutases." Annual Review of Biochemistry 64, no. 1 (1995): 97–112. http://dx.doi.org/10.1146/annurev.bi.64.070195.000525.

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33

Sheng, Yuewei, Isabel A. Abreu, Diane E. Cabelli, et al. "Superoxide Dismutases and Superoxide Reductases." Chemical Reviews 114, no. 7 (2014): 3854–918. http://dx.doi.org/10.1021/cr4005296.

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34

Rump, Alexis F. E., Renate Rösen, and Wolfgang Klaus. "Cardioprotection by Superoxide Dismutase." Anesthesia & Analgesia 76, no. 2 (1993): 239–46. http://dx.doi.org/10.1213/00000539-199302000-00007.

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35

WATANABE, KAZUTADA. "Superoxide Dismutase and Aging." Sen'i Gakkaishi 44, no. 5 (1988): P168—P173. http://dx.doi.org/10.2115/fiber.44.5_p168.

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36

Bowler, Chris, Wim Van Camp, Marc Van Montagu, Dirk Inzé, and Kozi Asada. "Superoxide Dismutase in Plants." Critical Reviews in Plant Sciences 13, no. 3 (1994): 199–218. http://dx.doi.org/10.1080/07352689409701914.

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37

Bowler, C., W. Van Camp, M. Van Montagu, and D. Inze. "Superoxide Dismutase in Plants." Critical Reviews in Plant Sciences 13, no. 3 (1994): 199. http://dx.doi.org/10.1080/713608062.

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38

Elmer, G. I., J. L. Evans, S. R. Goldberg, C. J. Epstein, and J. L. Cadet. "Transgenic superoxide dismutase mice." Behavioural Pharmacology 7, no. 7 (1996): 628???639. http://dx.doi.org/10.1097/00008877-199611000-00008.

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39

BORMAN, STU. "Superoxide dismutase mimic developed." Chemical & Engineering News 77, no. 41 (1999): 18. http://dx.doi.org/10.1021/cen-v077n041.p018.

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40

Orrell, RichardW, and JacquelineS deBelleroche. "Superoxide dismutase and ALS." Lancet 344, no. 8938 (1994): 1651–52. http://dx.doi.org/10.1016/s0140-6736(94)90452-9.

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41

Chen, Dan-Dan, and Alex F. Chen. "CuZn Superoxide Dismutase Deficiency." Hypertension 48, no. 6 (2006): 1026–28. http://dx.doi.org/10.1161/01.hyp.0000247304.56192.ce.

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42

Gillissen, Adrian, James H. Roum, Robert F. Hoyt, and Ronald G. Crystal. "Aerosolization of Superoxide Dismutase." Chest 104, no. 3 (1993): 811–15. http://dx.doi.org/10.1378/chest.104.3.811.

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43

Robinson, D. S., J. K. Donnelly, S. M. Lawlor, P. J. Frazier, and N. W. R. Daniels. "Wheat Superoxide Dismutase Isoenzymes." Journal of Cereal Science 23, no. 1 (1996): 93–101. http://dx.doi.org/10.1006/jcrs.1996.0009.

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44

Miller, Anne-Frances, K. Padmakumar, David L. Sorkin, A. Karapetian, and Carrie K. Vance. "Proton-coupled electron transfer in Fe-superoxide dismutase and Mn-superoxide dismutase." Journal of Inorganic Biochemistry 93, no. 1-2 (2003): 71–83. http://dx.doi.org/10.1016/s0162-0134(02)00621-9.

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45

Natvig, D. O., K. Imlay, D. Touati, and R. A. Hallewell. "Human copper-zinc superoxide dismutase complements superoxide dismutase-deficient Escherichia coli mutants." Journal of Biological Chemistry 262, no. 30 (1987): 14697–701. http://dx.doi.org/10.1016/s0021-9258(18)47851-9.

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46

Andersen, P. M., P. Nilsson, L. Forsgren, and S. L. Marklund. "CuZn-Superoxide Dismutase, Extracellular Superoxide Dismutase, and Glutathione Peroxidase in Blood from Individuals Homozygous for Asp90Ala CuZn-Superoxide Dismutase Mutation." Journal of Neurochemistry 70, no. 2 (2002): 715–20. http://dx.doi.org/10.1046/j.1471-4159.1998.70020715.x.

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47

Crosti, N., J. Bajer, A. Serra, A. Rigo, M. Scarpa, and P. Viglino. "Coordinate expression of Mn-containing superoxide dismutase and Cu,Zn-containing superoxide dismutase in human fibroblasts with trisomy 21." Journal of Cell Science 79, no. 1 (1985): 95–103. http://dx.doi.org/10.1242/jcs.79.1.95.

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The amount of Mn superoxide dismutase (MnSOD) and the activity of Cu,Zn-superoxide dismutase (CuZnSOD) have been studied in human fibroblasts of five subjects with trisomy 21 and five subjects with normal karyotype, using nuclear magnetic relaxation and polarographic methods. In the trisomic fibroblasts we have found a mean molar amount of MnSOD 25.4% lower than in the control, and an amount of CuZnSOD 54.7% higher. A positive significant correlation between the activities of both enzymes has been observed indicating that the two enzymes dismute the O2- cooperatively. However, the increase of

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48

Shin, Hyun Jae. "Effects of Swimming Exercise on Blood Leptin, Ghrelin, Superoxide Dismutase and Lipid Peroxidation in Obese Women." Journal of Sport and Leisure Studies 49 (August 31, 2012): 899–907. http://dx.doi.org/10.51979/kssls.2012.08.49.899.

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49

Giergiel, M., and M. Kankofer. "Age and sex-related changes in superoxide dismutase activity in bovine tissues." Czech Journal of Animal Science 60, No. 8 (2018): 367–74. http://dx.doi.org/10.17221/8406-cjas.

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The influence of age, gender, and type of tissue on superoxide dismutase (SOD) activity in bovine organs and tissues was investigated. The investigated material consisted of fragments of tissues and organs (liver, heart, lung, kidney, skeletal muscles, and diaphragm) from healthy cows (n = 15), bulls (n = 15), and female calves (n = 12) collected immediately after slaughter at the slaughterhouse. The total SOD activity was measured in tissue and organ homogenates by spectrophotometric method. PAGE electrophoresis and Western blotting technique with specific anti-SOD antibodies as well as zymog

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50

Campanella, Luigi, Gabriele Favero, and Mauro Tomassetti. "Superoxide Dismutase Biosensors for Superoxide Radical Analysis." Analytical Letters 32, no. 13 (1999): 2559–81. http://dx.doi.org/10.1080/00032719908542988.

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