메뉴 건너뛰기




Volumn 26, Issue 9, 2013, Pages 1312-1319

Superoxide dismutase mimics, other mimics, antioxidants, prooxidants, and related matters

(1)  Liochev, Stefan I a  

a NONE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIOXIDANT; CARBONIC ACID; FLAVOPROTEIN; GLUCOSE OXIDASE; HYDROXYL RADICAL; REACTIVE OXYGEN METABOLITE; SUPEROXIDE DISMUTASE; XANTHINE OXIDASE; BIOMIMETIC MATERIAL; FREE RADICAL; OXIDIZING AGENT;

EID: 84884219877     PISSN: 0893228X     EISSN: 15205010     Source Type: Journal    
DOI: 10.1021/tx4001623     Document Type: Article
Times cited : (14)

References (38)
  • 3
    • 79953791901 scopus 로고    scopus 로고
    • Cellular redox modulator, ortho Mn(III) meso-tetrakis(N-n- he5xylpyridinium-2-yl)porphyrin, MnTnHex-2-PyP(5+) in the treatment of brain tumors
    • Keir, S. T., Dewhirst, M. W., Kirkpatrick, J. P., Bigner, D. D., and Batinic-Haberle, I. (2011) Cellular redox modulator, ortho Mn(III) meso-tetrakis(N-n-he5xylpyridinium-2-yl)porphyrin, MnTnHex-2-PyP(5+) in the treatment of brain tumors Anticancer Agents Med. Chem. 11, 202-212
    • (2011) Anticancer Agents Med. Chem. , vol.11 , pp. 202-212
    • Keir, S.T.1    Dewhirst, M.W.2    Kirkpatrick, J.P.3    Bigner, D.D.4    Batinic-Haberle, I.5
  • 4
    • 77954735594 scopus 로고    scopus 로고
    • Superoxide dismutase mimics: Chemistry, pharmacology, and therapeutic potential
    • Batinic-Haberle, I., Reboucas, J. S., and Spasojevic, I. (2010) Superoxide dismutase mimics: chemistry, pharmacology, and therapeutic potential Antioxid. Redox Signaling 13, 877-918
    • (2010) Antioxid. Redox Signaling , vol.13 , pp. 877-918
    • Batinic-Haberle, I.1    Reboucas, J.S.2    Spasojevic, I.3
  • 6
    • 0027989826 scopus 로고
    • Stable Mn(III) porphyrins mimic superoxide dismutase in vitro and substitute for it in vivo
    • Faulkner, K. M., Liochev, S. I., and Fridovich, I. (1994) Stable Mn(III) porphyrins mimic superoxide dismutase in vitro and substitute for it in vivo J. Biol. Chem. 269, 23471-23476
    • (1994) J. Biol. Chem. , vol.269 , pp. 23471-23476
    • Faulkner, K.M.1    Liochev, S.I.2    Fridovich, I.3
  • 9
    • 0024227792 scopus 로고
    • The uniqueness of superoxide dismutase (SOD) - Why cannot most copper compounds substitute SOD in vivo?
    • Czapski, G. and Goldstein, S. (1988) The uniqueness of superoxide dismutase (SOD)-Why cannot most copper compounds substitute SOD in vivo? Free Radical Res. Commun. 4, 225-229
    • (1988) Free Radical Res. Commun. , vol.4 , pp. 225-229
    • Czapski, G.1    Goldstein, S.2
  • 10
    • 0023911964 scopus 로고
    • A critical reevaluation of some assay methods for superoxide dismutase activity
    • Goldstein, S., Michel, C., Bors, W., Saran, M., and Czapski, G. (1988) A critical reevaluation of some assay methods for superoxide dismutase activity Free Radical Biol. Med. 4, 295-303
    • (1988) Free Radical Biol. Med. , vol.4 , pp. 295-303
    • Goldstein, S.1    Michel, C.2    Bors, W.3    Saran, M.4    Czapski, G.5
  • 11
    • 33745829019 scopus 로고    scopus 로고
    • Reduction of manganese porphyrins by flavoenzymes and submitochondrial particles: A catalytic cycle for the reduction of peroxynitrite
    • Ferrer-Sueta, G., Hannibal, L., Batinic-Haberle, I., and Radi, R. (2006) Reduction of manganese porphyrins by flavoenzymes and submitochondrial particles: a catalytic cycle for the reduction of peroxynitrite Free Radical Biol. Med. 41, 503-512
    • (2006) Free Radical Biol. Med. , vol.41 , pp. 503-512
    • Ferrer-Sueta, G.1    Hannibal, L.2    Batinic-Haberle, I.3    Radi, R.4
  • 12
    • 0038707391 scopus 로고    scopus 로고
    • Mutant Cu,Zn superoxide dismutases and familial amyotrophic lateral sclerosis: Evaluation of oxidative hypotheses
    • Liochev, S. I. and Fridovich, I. (2003) Mutant Cu,Zn superoxide dismutases and familial amyotrophic lateral sclerosis: evaluation of oxidative hypotheses Free Radical Biol. Med. 34, 1383-1389
    • (2003) Free Radical Biol. Med. , vol.34 , pp. 1383-1389
    • Liochev, S.I.1    Fridovich, I.2
  • 13
    • 0024548679 scopus 로고
    • Effects of vanadate on the oxidation of NADH by xanthine oxidase
    • Liochev, S. I., Ivancheva, E., and Fridovich, I. (1989) Effects of vanadate on the oxidation of NADH by xanthine oxidase Arch. Biochem. Biophys. 269, 188-193
    • (1989) Arch. Biochem. Biophys. , vol.269 , pp. 188-193
    • Liochev, S.I.1    Ivancheva, E.2    Fridovich, I.3
  • 14
    • 18144396884 scopus 로고    scopus 로고
    • A novel class of cytochrome P450 reductase redox cyclers: Cationic manganoporphyrins
    • Day, B. J. and Kariya, C. (2005) A novel class of cytochrome P450 reductase redox cyclers: Cationic manganoporphyrins Toxicol. Sci. 85, 713-719
    • (2005) Toxicol. Sci. , vol.85 , pp. 713-719
    • Day, B.J.1    Kariya, C.2
  • 15
    • 0028965665 scopus 로고
    • Superoxide from glucose oxidase or from nitroblue tetrazolium?
    • Liochev, S. I. and Fridovich, I. (1995) Superoxide from glucose oxidase or from nitroblue tetrazolium? Arch. Biochem. Biophys. 318, 408-410
    • (1995) Arch. Biochem. Biophys. , vol.318 , pp. 408-410
    • Liochev, S.I.1    Fridovich, I.2
  • 16
    • 0029116075 scopus 로고
    • A cationic manganic porphyrin inhibits uptake of paraquat by Escherichia coli
    • Liochev, S. I. and Fridovich, I. (1995) A cationic manganic porphyrin inhibits uptake of paraquat by Escherichia coli Arch. Biochem. Biophys. 321, 271-275
    • (1995) Arch. Biochem. Biophys. , vol.321 , pp. 271-275
    • Liochev, S.I.1    Fridovich, I.2
  • 17
    • 0020118402 scopus 로고
    • The scavenging of superoxide radical by manganous complexes: In vitro
    • Archibald, F. S. and Fridovich, I. (1982) The scavenging of superoxide radical by manganous complexes: in vitro Arch. Biochem. Biophys. 214, 452-463
    • (1982) Arch. Biochem. Biophys. , vol.214 , pp. 452-463
    • Archibald, F.S.1    Fridovich, I.2
  • 18
    • 4344651232 scopus 로고    scopus 로고
    • Carbon dioxide mediates Mn(II)-catalyzed decomposition of hydrogen peroxide and peroxidation reactions
    • Liochev, S. I. and Fridovich, I. (2004) Carbon dioxide mediates Mn(II)-catalyzed decomposition of hydrogen peroxide and peroxidation reactions Proc. Natl. Acad. Sci. U.S.A. 101, 12485-12490
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 12485-12490
    • Liochev, S.I.1    Fridovich, I.2
  • 19
    • 84860798289 scopus 로고    scopus 로고
    • Biologically relevant mechanism for catalytic superoxide removal by simple manganese compounds
    • Barnese, K., Gralla, E. B., Valentine, J. S., and Cabelli, D. E. (2012) Biologically relevant mechanism for catalytic superoxide removal by simple manganese compounds Proc. Natl. Acad. Sci. U.S.A. 109, 6892-6897
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 6892-6897
    • Barnese, K.1    Gralla, E.B.2    Valentine, J.S.3    Cabelli, D.E.4
  • 20
    • 22444444422 scopus 로고    scopus 로고
    • A pulse radiolysis study of catalytic superoxide radical dismutation by a manganese(II) complex with an N-tripodal ligand
    • Durot, S., Lambert, F. L., Renault, J.-P., and Policar, C. (2005) A pulse radiolysis study of catalytic superoxide radical dismutation by a manganese(II) complex with an N-tripodal ligand Eur. J. Inorg. Chem. 14, 2789-2793
    • (2005) Eur. J. Inorg. Chem. , vol.14 , pp. 2789-2793
    • Durot, S.1    Lambert, F.L.2    Renault, J.-P.3    Policar, C.4
  • 22
    • 34247109461 scopus 로고    scopus 로고
    • The effects of superoxide dismutase on H2O2 formation
    • Liochev, S. I. and Fridovich, I. (2007) The effects of superoxide dismutase on H2O2 formation Free Radical Biol. Med. 42, 1465-1469
    • (2007) Free Radical Biol. Med. , vol.42 , pp. 1465-1469
    • Liochev, S.I.1    Fridovich, I.2
  • 23
    • 84874931751 scopus 로고    scopus 로고
    • Reactive oxygen species and the free radical theory of aging
    • Liochev, S. I. (2013) Reactive oxygen species and the free radical theory of aging Free Radical Biol. Med. 60, 1-4
    • (2013) Free Radical Biol. Med. , vol.60 , pp. 1-4
    • Liochev, S.I.1
  • 24
  • 25
    • 84877992025 scopus 로고    scopus 로고
    • Differential coordination demands in fe versus mn water-soluble cationic metalloporphyrins translate into remarkably different aqueous redox chemistry and biology
    • Tovmasyan, A., Weitner, T., Sheng, H., Lu, M., Rajic, Z., Warner, D. S., Spasojevic, I., Reboucas, J. S., Benov, L., and Batinic-Haberle, I. (2013) Differential coordination demands in fe versus mn water-soluble cationic metalloporphyrins translate into remarkably different aqueous redox chemistry and biology Inorg. Chem. 52, 5677-5691
    • (2013) Inorg. Chem. , vol.52 , pp. 5677-5691
    • Tovmasyan, A.1    Weitner, T.2    Sheng, H.3    Lu, M.4    Rajic, Z.5    Warner, D.S.6    Spasojevic, I.7    Reboucas, J.S.8    Benov, L.9    Batinic-Haberle, I.10
  • 26
    • 84856564249 scopus 로고    scopus 로고
    • Mitochondrial oxidative stress and epilepsy in SOD2 deficient mice: Attenuation by a lipophilic metalloporphyrin
    • Liang, L. P., Waldbaum, S., Rowley, S., Huang, T. T., Day, B. J., and Patel, M. (2012) Mitochondrial oxidative stress and epilepsy in SOD2 deficient mice: attenuation by a lipophilic metalloporphyrin Neurobiol. Dis. 45, 1068-1076
    • (2012) Neurobiol. Dis. , vol.45 , pp. 1068-1076
    • Liang, L.P.1    Waldbaum, S.2    Rowley, S.3    Huang, T.T.4    Day, B.J.5    Patel, M.6
  • 28
    • 1242316151 scopus 로고    scopus 로고
    • Mitochondrial oxidative stress and increased seizure susceptibility in Sod2(-/+) mice
    • Liang, L. P. and Patel, M. (2004) Mitochondrial oxidative stress and increased seizure susceptibility in Sod2(-/+) mice Free Radical. Biol. Med. 36, 542-554
    • (2004) Free Radical. Biol. Med. , vol.36 , pp. 542-554
    • Liang, L.P.1    Patel, M.2
  • 30
    • 84890434912 scopus 로고    scopus 로고
    • Does MitoSOD protect against the toxicity of paraquat toward mitochondria by acting as a superoxide dismutase mimic?
    • [Online early access], DOI: 10.1016/j.freeradbiomed.2013.02.010. published online: Feb 19, 2013, (accessed Apr 22, 2013).
    • Liochev, S. I. and Fridovich, I. (2013) Does MitoSOD protect against the toxicity of paraquat toward mitochondria by acting as a superoxide dismutase mimic? Free Radical Biol. Med. [Online early access], DOI: 10.1016/j. freeradbiomed.2013.02.010., published online: Feb 19, 2013, http://dx.doi.org/ 10.1016/j.freeradbiomed.2013.02.010 (accessed Apr 22, 2013).
    • (2013) Free Radical Biol. Med.
    • Liochev, S.I.1    Fridovich, I.2
  • 31
    • 0025768952 scopus 로고
    • Effects of overproduction of superoxide dismutase on the toxicity of paraquat toward Escherichia coli
    • Liochev, S. I and Fridovich, I. (1991) Effects of overproduction of superoxide dismutase on the toxicity of paraquat toward Escherichia coli J. Biol. Chem. 266, 8747-8750
    • (1991) J. Biol. Chem. , vol.266 , pp. 8747-8750
    • Liochev, S.I.1    Fridovich, I.2
  • 32
    • 0026594013 scopus 로고
    • Effects of overproduction of superoxide dismutases in Escherichia coli on inhibition of growth and on induction of glucose-6-phosphate dehydrogenase by paraquat
    • Liochev, S. I. and Fridovich, I. (1992) Effects of overproduction of superoxide dismutases in Escherichia coli on inhibition of growth and on induction of glucose-6-phosphate dehydrogenase by paraquat Arch. Biochem. Biophys. 294, 138-143
    • (1992) Arch. Biochem. Biophys. , vol.294 , pp. 138-143
    • Liochev, S.I.1    Fridovich, I.2
  • 33
    • 43149105201 scopus 로고    scopus 로고
    • Rapid changes in gene expression dynamics in response to superoxide reveal SoxRS-dependent and -independent transcriptional networks
    • Blanchard, J. L., Wholely, W. Y., Conlon, E. M., and Pomposiello, P. J. (2007) Rapid changes in gene expression dynamics in response to superoxide reveal SoxRS-dependent and -independent transcriptional networks PLoS One 2, e1186
    • (2007) PLoS One , vol.2 , pp. 1186
    • Blanchard, J.L.1    Wholely, W.Y.2    Conlon, E.M.3    Pomposiello, P.J.4
  • 34
    • 0034977251 scopus 로고    scopus 로고
    • Genome-wide transcriptional profiling of the Escherichia coli responses to superoxide stress and sodium salicylate
    • Pomposiello, P. J., Bennik, M. H., and Demple, B. (2001) Genome-wide transcriptional profiling of the Escherichia coli responses to superoxide stress and sodium salicylate J. Bacteriol. 183, 3890-3902
    • (2001) J. Bacteriol. , vol.183 , pp. 3890-3902
    • Pomposiello, P.J.1    Bennik, M.H.2    Demple, B.3
  • 35
    • 84872159740 scopus 로고    scopus 로고
    • Upregulation of phase II enzymes through phytochemical activation of NRF2 protects cardiomyocytes against oxidative stress
    • Reuland, D. J., Khademi, S., Castle, C. J., Irwin, D. C., McCord, J. M., Miller, B. F., and Hamilton, K. L. (2013) Upregulation of phase II enzymes through phytochemical activation of NRF2 protects cardiomyocytes against oxidative stress Free Radical Biol. Med. 56, 102-111
    • (2013) Free Radical Biol. Med. , vol.56 , pp. 102-111
    • Reuland, D.J.1    Khademi, S.2    Castle, C.J.3    Irwin, D.C.4    McCord, J.M.5    Miller, B.F.6    Hamilton, K.L.7
  • 36
    • 84892373466 scopus 로고    scopus 로고
    • Regulation of Nrf2 - An update
    • [Online early access], DOI: 10.1016/j.freeradbiomed.2013.02.008, published online: Feb 19, 2013, (accessed Apr 22, 2013).
    • Niture, S. K., Khatri, R., and Jaiswal, A. K. (2013) Regulation of Nrf2-an update. Free Radical Biol. Med. [Online early access], DOI: 10.1016/j.freeradbiomed.2013.02.008, published online: Feb 19, 2013, http://dx.doi.org/10.1016/j.freeradbiomed.2013.02.008 (accessed Apr 22, 2013).
    • (2013) Free Radical Biol. Med.
    • Niture, S.K.1    Khatri, R.2    Jaiswal, A.K.3
  • 37
    • 84860331697 scopus 로고    scopus 로고
    • Free radicals and antioxidants: Updating a personal view
    • Halliwell, B. (2012) Free radicals and antioxidants: updating a personal view Nutr. Rev. 70, 257-65
    • (2012) Nutr. Rev. , vol.70 , pp. 257-265
    • Halliwell, B.1
  • 38
    • 84892370999 scopus 로고    scopus 로고
    • Organochalcogen peroxidase mimetics as potential drugs: A long story of a promise still unfulfilled
    • [Online early access], DOI: 10.1016/j.freeradbiomed.2013.03.006, published online: Mar 14, 2013, (accessed Apr 22, 2013).
    • Orian, L. and Toppo, S. (2013) Organochalcogen peroxidase mimetics as potential drugs: a long story of a promise still unfulfilled. Free Radical Biol. Med. [Online early access], DOI: 10.1016/j.freeradbiomed.2013.03.006, published online: Mar 14, 2013, http://dx.doi.org/10.1016/j.freeradbiomed.2013.03.006 (accessed Apr 22, 2013).
    • (2013) Free Radical Biol. Med.
    • Orian, L.1    Toppo, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.