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Volumn 20, Issue 2, 2014, Pages 155-160

Hydrogen peroxide produced by mitochondrial monoamine oxidase catalysis: Biological implications

Author keywords

Amine oxidation; Hydrogen peroxide; Hydroxyl radical; Membrane topology; Mitochondrial intermembrane space; Mitochondrial outer membrane; Monoamine oxidases A and B; Reactive oxygen species

Indexed keywords

AMINE OXIDASE (FLAVIN CONTAINING) ISOENZYME A; AMINE OXIDASE (FLAVIN CONTAINING) ISOENZYME B; HYDROGEN PEROXIDE; HYDROXYL RADICAL; MONOAMINE OXIDASE INHIBITOR; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); SUPEROXIDE; UBIQUINOL CYTOCHROME C REDUCTASE;

EID: 84893021427     PISSN: 13816128     EISSN: 18734286     Source Type: Journal    
DOI: 10.2174/13816128113190990406     Document Type: Article
Times cited : (138)

References (48)
  • 1
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • Murphy MP. How mitochondria produce reactive oxygen species. Biochem J 2009; 417: 1-13.
    • (2009) Biochem J , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 2
    • 84868007565 scopus 로고    scopus 로고
    • Physiological Roles of Mitochondrial Reactive Oxygen Species
    • Sena LA, Chandel NS. Physiological Roles of Mitochondrial Reactive Oxygen Species. Molec Cell 2012; 48: 158-431.
    • (2012) Molec Cell , vol.48 , pp. 158-431
    • Sena, L.A.1    Chandel, N.S.2
  • 3
    • 0030768730 scopus 로고    scopus 로고
    • Age-related increases in brain monoamine oxidase B in living healthy human subjects
    • Fowler JS, Volkow ND, Wang GJ, et al. Age-related increases in brain monoamine oxidase B in living healthy human subjects. Neurobiol Aging 1997; 18: 431-5.
    • (1997) Neurobiol Aging , vol.18 , pp. 431-435
    • Fowler, J.S.1    Volkow, N.D.2    Wang, G.J.3
  • 4
    • 0032976196 scopus 로고    scopus 로고
    • Reactive oxygen species production by monoamine oxidases in intact cells
    • Pizzinat N, Copin N, Vindis C, Parini A, Cambon C. Reactive oxygen species production by monoamine oxidases in intact cells. N-S Arch Pharmacol 1999; 359: 428-31.
    • (1999) N-S Arch Pharmacol , vol.359 , pp. 428-431
    • Pizzinat, N.1    Copin, N.2    Vindis, C.3    Parini, A.4    Cambon, C.5
  • 5
    • 79953762174 scopus 로고    scopus 로고
    • Unraveling the Biological Roles of Reactive Oxygen Species
    • Murphy MP, Holmgren A, Larsson NG, et al. Unraveling the Biological Roles of Reactive Oxygen Species. Cell Metab 2011; 13: 361-6.
    • (2011) Cell Metab , vol.13 , pp. 361-366
    • Murphy, M.P.1    Holmgren, A.2    Larsson, N.G.3
  • 6
    • 0025871857 scopus 로고
    • Kinetic Mechanism of Monoamine Oxidase A
    • Ramsay RR. Kinetic Mechanism of Monoamine Oxidase A. Biochemistry 1991; 30: 4624-9.
    • (1991) Biochemistry , vol.30 , pp. 4624-4629
    • Ramsay, R.R.1
  • 7
    • 0033773601 scopus 로고    scopus 로고
    • High Level Expression of Human Liver Monoamine Oxidase B in Pichia pastoris
    • Newton-Vinson, P, Hubalek F, Edmondson DE. High Level Expression of Human Liver Monoamine Oxidase B in Pichia pastoris. Prot Expr Purif 2000; 20: 334-45.
    • (2000) Prot Expr Purif , vol.20 , pp. 334-345
    • Newton-Vinson, P.1    Hubalek, F.2    Edmondson, D.E.3
  • 8
    • 0024673117 scopus 로고
    • Human monoamine oxidase A and B genes map to Xp 11. 23 and are deleted in a patient with Norrie disease
    • Lan NC, Heinzmann C, Gal A, et al. Human monoamine oxidase A and B genes map to Xp 11. 23 and are deleted in a patient with Norrie disease. Genomics 1989; 4: 552-9.
    • (1989) Genomics , vol.4 , pp. 552-559
    • Lan, N.C.1    Heinzmann, C.2    Gal, A.3
  • 9
    • 66149173641 scopus 로고    scopus 로고
    • Molecular and Mechanistic Properties of the Membrane-Bound Mitochondrial Monoamine Oxidases
    • Edmondson DE, Binda C, Wang J, Upadhyay A, Mattevi A. Molecular and Mechanistic Properties of the Membrane-Bound Mitochondrial Monoamine Oxidases. Biochemistry 2009; 48: 4220-30.
    • (2009) Biochemistry , vol.48 , pp. 4220-4230
    • Edmondson, D.E.1    Binda, C.2    Wang, J.3    Upadhyay, A.4    Mattevi, A.5
  • 10
    • 80051489294 scopus 로고    scopus 로고
    • Monoamine Oxidase A Expression is Vital for Embryonic Brain Development by Modulating Developmental Apoptosis
    • Wang CC, Borchert A, Ugam-Klusek A, et al. Monoamine Oxidase A Expression is Vital for Embryonic Brain Development by Modulating Developmental Apoptosis. J Biol Chem 2011; 286 28322-30.
    • (2011) J Biol Chem , vol.286 , pp. 28322-283230
    • Wang, C.C.1    Borchert, A.2    Ugam-Klusek, A.3
  • 11
    • 0035996741 scopus 로고    scopus 로고
    • High-Level Expression of Human Monoamine Oxidase A in Pichia pastoris: Comparison with the Enzyme Expressed in Saccharomyces cerevisiae
    • Li M, Hubalek, F, Newton-Vinson, P. Edmondson DE. High-Level Expression of Human Monoamine Oxidase A in Pichia pastoris: Comparison with the Enzyme Expressed in Saccharomyces cerevisiae. Prot Expr Purif 2002; 24: 152-62.
    • (2002) Prot Expr Purif , vol.24 , pp. 152-162
    • Li, M.1    Hubalek, F.2    Newton-Vinson, P.3    Edmondson, D.E.4
  • 12
    • 0036140732 scopus 로고    scopus 로고
    • Structure of human monoamine oxidase B, a drug target for the treatment of neurological disorders
    • Binda, C, Newton-Vinson P, Hubalek F, Edmondson DE, Mattevi A. Structure of human monoamine oxidase B, a drug target for the treatment of neurological disorders. Nat Struct Biol 2002; 9: 22-6.
    • (2002) Nat Struct Biol , vol.9 , pp. 22-26
    • Binda, C.1    Newton-Vinson, P.2    Hubalek, F.3    Edmondson, D.E.4    Mattevi, A.5
  • 13
    • 24644437716 scopus 로고    scopus 로고
    • Three-dimensional structure of human monoamine oxidase A (MAO A): Relation to the structures of rat MAO A and human MAO B
    • DeColibus L, Li M, Binda C, et al. Three-dimensional structure of human monoamine oxidase A (MAO A): relation to the structures of rat MAO A and human MAO B. Proc Natl Acad Sci USA 2005; 102: 12684-9.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 12684-12689
    • DeColibus, L.1    Li, M.2    Binda, C.3
  • 14
    • 44449117421 scopus 로고    scopus 로고
    • Structure of human monoamine oxidase A at 2. 2 angstrom resolution: The control of opening the entry for substrates/inhibitors
    • Son SY, Ma J, Kondou Y, Yoshimura M, Yamashita E, Tsukihara T. Structure of human monoamine oxidase A at 2. 2 angstrom resolution: the control of opening the entry for substrates/inhibitors. Proc Natl Sci USA 2008; 105: 5739-44.
    • (2008) Proc Natl Sci USA , vol.105 , pp. 5739-5744
    • Son, S.Y.1    Ma, J.2    Kondou, Y.3    Yoshimura, M.4    Yamashita, E.5    Tsukihara, T.6
  • 15
    • 1842474296 scopus 로고    scopus 로고
    • Structure of Rat Monoamine Oxidase A and Its Specific Recognitions for Substrates and Inhibitors
    • Ma J, Yoshimura M, Yamashita E, Nakagawa A, Ito A, Tsukihara T. Structure of Rat Monoamine Oxidase A and Its Specific Recognitions for Substrates and Inhibitors. J Mol Biol 2004; 338: 103-14.
    • (2004) J Mol Biol , vol.338 , pp. 103-114
    • Ma, J.1    Yoshimura, M.2    Yamashita, E.3    Nakagawa, A.4    Ito, A.5    Tsukihara, T.6
  • 16
    • 38949096792 scopus 로고    scopus 로고
    • Determination of the Oligomeric States of Human and Rat Monoamine Oxidases in the Outer Mitochondrial Membrane and Octyl r-D-Glucopyranoside Micelles Using Pulsed Dipolar Electron Spin Resonance Spectroscopy
    • Upadhyay A, Borbat PP, Wang J, Freed, JH, Edmondson DE. Determination of the Oligomeric States of Human and Rat Monoamine Oxidases in the Outer Mitochondrial Membrane and Octyl r-D-Glucopyranoside Micelles Using Pulsed Dipolar Electron Spin Resonance Spectroscopy. Biochemistry 2008; 47: 1554-66.
    • (2008) Biochemistry , vol.47 , pp. 1554-1566
    • Upadhyay, A.1    Borbat, P.P.2    Wang, J.3    Freed, J.H.4    Edmondson, D.E.5
  • 17
    • 34547937485 scopus 로고    scopus 로고
    • How tails guide tailanchored proteins to their destinations
    • Borgese N, Brambillasca S, Colombo S. How tails guide tailanchored proteins to their destinations. Curr Opin Cell Biol 2007; 19: 368-75.
    • (2007) Curr Opin Cell Biol , vol.19 , pp. 368-375
    • Borgese, N.1    Brambillasca, S.2    Colombo, S.3
  • 18
    • 84865435786 scopus 로고    scopus 로고
    • The enigmatic reaction of flavins with oxygen
    • Chaiyen P, Fraaije MW, Mattevi A. The enigmatic reaction of flavins with oxygen. Tr Biochem Sci 2012; 37: 373-80.
    • (2012) Tr Biochem Sci , vol.37 , pp. 373-380
    • Chaiyen, P.1    Fraaije, M.W.2    Mattevi, A.3
  • 19
    • 0003636920 scopus 로고    scopus 로고
    • High level Expression, Structural, Kinetic, and Redox Characterization of Recombinant Human Liver Monoamine Oxidase B
    • In: Ghisla S, Kroneck P, Macheroux P, Sund H, Eds, Rudolf Weber. Berlin: Agency for Scientific Publications
    • Newton-Vinson P, Edmondson DE. High level Expression, Structural, Kinetic, and Redox Characterization of Recombinant Human Liver Monoamine Oxidase B. In: Ghisla S, Kroneck P, Macheroux P, Sund H, Eds. Flavins and Flavoproteins. Rudolf Weber. Berlin: Agency for Scientific Publications 1999; pp. 431-4.
    • (1999) Flavins and Flavoproteins , pp. 431-434
    • Newton-Vinson, P.1    Edmondson, D.E.2
  • 20
    • 33748638376 scopus 로고    scopus 로고
    • The equilibrium between the oxidation of hydrogen peroxide by oxygen and the dismutation of peoxyl or superoxide radicals in aqueous solutions in contact with oxygen
    • Petlicki J, van de Ven TGM. The equilibrium between the oxidation of hydrogen peroxide by oxygen and the dismutation of peoxyl or superoxide radicals in aqueous solutions in contact with oxygen. J Chem Soc Faraday Trans 1998; 94: 2763-7.
    • (1998) J Chem Soc Faraday Trans , vol.94 , pp. 2763-2767
    • Petlicki, J.1    van de Ven, T.G.M.2
  • 21
    • 0002256757 scopus 로고
    • The Fitness of Oxygen
    • In: King TE, Mason HS, Morrison M, Eds, J Wiley New York
    • George, P. The Fitness of Oxygen. In: King TE, Mason HS, Morrison M, Eds. Oxidases and Related Redox Systems. J Wiley New York 1965; pp. 15-23.
    • (1965) Oxidases and Related Redox Systems , pp. 15-23
    • George, P.1
  • 22
    • 0018496663 scopus 로고
    • The vectorial orientation of human monoamine oxidase in mitochondrial outer membrane
    • Russell SM, Davey J, Mayer RJ. The vectorial orientation of human monoamine oxidase in mitochondrial outer membrane. Biochem J 1979; 181: 7-14.
    • (1979) Biochem J , vol.181 , pp. 7-14
    • Russell, S.M.1    Davey, J.2    Mayer, R.J.3
  • 23
    • 0021350521 scopus 로고
    • Proteases as probes of mitochondrial monoamine oxidase topography in situ
    • Buckman TD, Sutphin MS, Eiduson S, Proteases as probes of mitochondrial monoamine oxidase topography in situ. Molec Pharmacol 1984; 25: 165-70.
    • (1984) Molec Pharmacol , vol.25 , pp. 165-170
    • Buckman, T.D.1    Sutphin, M.S.2    Eiduson, S.3
  • 24
    • 0026071272 scopus 로고
    • Intramitochondrial formation of oxidized glutathione during the oxidation of benzylamine by monoamine oxidase
    • Werner P, Cohen G. Intramitochondrial formation of oxidized glutathione during the oxidation of benzylamine by monoamine oxidase. FEBS Lett 1991; 280: 44-6.
    • (1991) FEBS Lett , vol.280 , pp. 44-46
    • Werner, P.1    Cohen, G.2
  • 25
    • 79953214910 scopus 로고    scopus 로고
    • Topological Probes of Monoamine Oxidases A and B in Rat Liver Mitochondria: Inhibition by TEMPOSubstituted Pargyline Analogues and Inactivation by Proteolysis
    • Wang J, Edmondson DE. Topological Probes of Monoamine Oxidases A and B in Rat Liver Mitochondria: Inhibition by TEMPOSubstituted Pargyline Analogues and Inactivation by Proteolysis. Biochemistry 2011; 50: 2499-505.
    • (2011) Biochemistry , vol.50 , pp. 2499-2505
    • Wang, J.1    Edmondson, D.E.2
  • 26
    • 66149127694 scopus 로고    scopus 로고
    • Development of Spin-Labeled Pargyline Analogues as Specific Inhibitors of Human Monoamine Oxidases A and B
    • Upadhyay AK, Edmondson DE. Development of Spin-Labeled Pargyline Analogues as Specific Inhibitors of Human Monoamine Oxidases A and B. Biochemistry 2009; 48: 3928-35.
    • (2009) Biochemistry , vol.48 , pp. 3928-3935
    • Upadhyay, A.K.1    Edmondson, D.E.2
  • 27
    • 84863286462 scopus 로고    scopus 로고
    • Magnetic nanoparticles: An improved method for mitochondrial isolation
    • Tang B, Zhao, L, Liang R, Zhang Y, Wang L. Magnetic nanoparticles: An improved method for mitochondrial isolation. Molec Med Repts 2012; 5: 1271-6.
    • (2012) Molec Med Repts , vol.5 , pp. 1271-1276
    • Tang, B.1    Zhao, L.2    Liang, R.3    Zhang, Y.4    Wang, L.5
  • 28
    • 0030589009 scopus 로고    scopus 로고
    • The Metabolism of Tyramine by Monoamine Oxidase A/B Causes Oxidative Damage to Mitochondrial DNA
    • Hauptman N, Grimsby J, Shih JC, Cadenas E. The Metabolism of Tyramine by Monoamine Oxidase A/B Causes Oxidative Damage to Mitochondrial DNA. Arch Biochem Biophys 1996; 335: 295-304.
    • (1996) Arch Biochem Biophys , vol.335 , pp. 295-304
    • Hauptman, N.1    Grimsby, J.2    Shih, J.C.3    Cadenas, E.4
  • 29
    • 0344443765 scopus 로고    scopus 로고
    • Oxidative r-Ketoglutarate Dehydrogenase Inhibition via Subtle Elevations in Monoamine Oxidase B Levels Results in Loss of Spare Respiratory Capacity. Implications for Parkinson's Disease
    • Kumar MJ, Nicholls DG, Andersen JK. Oxidative r-Ketoglutarate Dehydrogenase Inhibition via Subtle Elevations in Monoamine Oxidase B Levels Results in Loss of Spare Respiratory Capacity. Implications for Parkinson's Disease. J Biol Chem 2003; 278: 46432-9.
    • (2003) J Biol Chem , vol.278 , pp. 46432-46439
    • Kumar, M.J.1    Nicholls, D.G.2    Andersen, J.K.3
  • 31
    • 33644874936 scopus 로고    scopus 로고
    • Oxidative stress by Monoamine Oxidase Mediates Receptor-Independent Cardiomyocyte Apoptosis by Serotonin and Postischemic Myocardial Injury
    • Bianchi P, Kunduzova O, Masini E, et al. Oxidative stress by Monoamine Oxidase Mediates Receptor-Independent Cardiomyocyte Apoptosis by Serotonin and Postischemic Myocardial Injury. Circulation 2005; 112: 3297-305.
    • (2005) Circulation , vol.112 , pp. 3297-3305
    • Bianchi, P.1    Kunduzova, O.2    Masini, E.3
  • 32
    • 0037377592 scopus 로고    scopus 로고
    • Age-dependent increase in hydrogen peroxide production by cardiac monoamine oxidase A in rats
    • Maurel, A, Hernandez C, Kunduzova O, et al. Age-dependent increase in hydrogen peroxide production by cardiac monoamine oxidase A in rats. Am J Physiol Heart Circ Physiol 2003; 284: H1460-H1467.
    • (2003) Am J Physiol Heart Circ Physiol , vol.284
    • Maurel, A.1    Hernandez, C.2    Kunduzova, O.3
  • 33
    • 61749092853 scopus 로고    scopus 로고
    • Genetic deletion of MAO-A promotes serotonin-dependent ventricular hypertrophy by pressure overload. J
    • Lairez O, Calise D, Bianchi P, et al. Genetic deletion of MAO-A promotes serotonin-dependent ventricular hypertrophy by pressure overload. J. Molec Cell Cardiol 2009; 46: 587-95.
    • (2009) Molec Cell Cardiol , vol.46 , pp. 587-595
    • Lairez, O.1    Calise, D.2    Bianchi, P.3
  • 35
    • 67349085802 scopus 로고    scopus 로고
    • Role of hydrogen peroxide and the impact of glutathione peroxidase-1 in regulation of cerebral vascular tone. J
    • Modrick MI, Didion SP, Lynch CM, Dayal S, Lenz SR, Faraci FM. Role of hydrogen peroxide and the impact of glutathione peroxidase-1 in regulation of cerebral vascular tone. J. Cereb Blood Flow Metab 2009; 29: 1130-7.
    • (2009) Cereb Blood Flow Metab , vol.29 , pp. 1130-1137
    • Modrick, M.I.1    Didion, S.P.2    Lynch, C.M.3    Dayal, S.4    Lenz, S.R.5    Faraci, F.M.6
  • 37
    • 77958586636 scopus 로고    scopus 로고
    • Mitochondrial monoamine oxidase-A-mediated hydrogen peroxide generation enhances 5-hydroxytryptamine-induced contraction of rat basilar artery
    • Poon CCW, Seto SW, Shan-Au AL, et al. Mitochondrial monoamine oxidase-A-mediated hydrogen peroxide generation enhances 5-hydroxytryptamine-induced contraction of rat basilar artery. Br J Pharmacol 2010; 161: 1086-98.
    • (2010) Br J Pharmacol , vol.161 , pp. 1086-1098
    • Poon, C.C.W.1    Seto, S.W.2    Shan-Au, A.L.3
  • 38
    • 84893005053 scopus 로고
    • In: Palmer GC, Ed. Neuropharmacology of Central Nervous System and Behavioural Disorders. Academic Press. New York
    • MacCauley RB Monoamine oxidase and the pharmacology of monoamine oxidase inhibitors. In: Palmer GC. Ed. Neuropharmacology of Central Nervous System and Behavioural Disorders. Academic Press. New York 1980; pp. 1130-7.
    • (1980) Monoamine oxidase and the pharmacology of monoamine oxidase inhibitors , pp. 1130-1137
    • McCauley, R.B.1
  • 39
    • 70449301912 scopus 로고
    • Amine Oxidase Inhibitors: Their Current Place in the Therapy of Cardiovascular Diseases
    • Griffith GC. Amine Oxidase Inhibitors: Their Current Place in the Therapy of Cardiovascular Diseases. Circulation 1960; 22: 1156-65.
    • (1960) Circulation , vol.22 , pp. 1156-1165
    • Griffith, G.C.1
  • 40
    • 43949123265 scopus 로고    scopus 로고
    • Structural and Mechanistic Studies of Arylalkylhydrazine Inhibition of Human Monoamine Oxidases A and B
    • Binda C, Li M, Hubalek F, Mattevi A, Edmondson DE. Structural and Mechanistic Studies of Arylalkylhydrazine Inhibition of Human Monoamine Oxidases A and B. Biochemistry 2008; 47: 5616-25.
    • (2008) Biochemistry , vol.47 , pp. 5616-5625
    • Binda, C.1    Li, M.2    Hubalek, F.3    Mattevi, A.4    Edmondson, D.E.5
  • 41
    • 84863664040 scopus 로고    scopus 로고
    • Perinuclear Mitochondrial Clustering Creates an Oxidant-Rich Nuclear Domain Required for Hypoxia-Induced Transcription
    • ra47 [DOI 10. 1126/scisignal. 2002712]
    • Al-Mehdi A-B, Pastukh VM, Swiger BM, et al. Perinuclear Mitochondrial Clustering Creates an Oxidant-Rich Nuclear Domain Required for Hypoxia-Induced Transcription. Science Signal 2012; 5 (231) ra47 [DOI: 10. 1126/scisignal. 2002712].
    • (2012) Science Signal , vol.5 , Issue.231
    • Al-Mehdi, A.-B.1    Pastukh, V.M.2    Swiger, B.M.3
  • 42
    • 33847753534 scopus 로고    scopus 로고
    • Specific Aquaporins Facilitate the Diffusion of Hydrogen Peroxide across Membranes
    • Bienert GP, Moller ALB, Kristiansen KA, et al. Specific Aquaporins Facilitate the Diffusion of Hydrogen Peroxide across Membranes. J Biol Chem 2007; 282: 1183-92.
    • (2007) J Biol Chem , vol.282 , pp. 1183-1192
    • Bienert, G.P.1    Moller, A.L.B.2    Kristiansen, K.A.3
  • 43
    • 77957652745 scopus 로고    scopus 로고
    • Aquaporin-3 mediates hydrogen peroxide uptake to regulate downstream intracellular signaling
    • Miller EW, Dickinson BC, Chang CJ. Aquaporin-3 mediates hydrogen peroxide uptake to regulate downstream intracellular signaling. Proc Natl Acad Sci USA 2010; 107: 15681-6.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 15681-15686
    • Miller, E.W.1    Dickinson, B.C.2    Chang, C.J.3
  • 44
    • 84866873131 scopus 로고    scopus 로고
    • Mitochondrial aquaporin-8 knockdown in human hepatoma HepG2 cells causes ROS-induced mitochondrial depolarization and loss of viability
    • Marchissio MJ, Eleazar, D, Frances, A., carnovale, CE, Marinelli RA. Mitochondrial aquaporin-8 knockdown in human hepatoma HepG2 cells causes ROS-induced mitochondrial depolarization and loss of viability. Toxicol Appl Pharmacol 2012; 264: 246-54.
    • (2012) Toxicol Appl Pharmacol , vol.264 , pp. 246-254
    • Marchissio, M.J.1    Eleazar, D.2    Frances, A.3    carnovale, C.E.4    Marinelli, R.A.5
  • 45
    • 33745206921 scopus 로고    scopus 로고
    • Evidence against Functionally Significant Aquaporin Expression in Mitochondria
    • Yang B, Zhao D, Verkman AS. Evidence against Functionally Significant Aquaporin Expression in Mitochondria. J Biol Chem 2006; 281: 16202-6.
    • (2006) J Biol Chem , vol.281 , pp. 16202-16206
    • Yang, B.1    Zhao, D.2    Verkman, A.S.3
  • 47
    • 77957060561 scopus 로고    scopus 로고
    • The Intermembrane Space of Mitochondria
    • Herrmann JM, Reimer J. The Intermembrane Space of Mitochondria. Antiox Redox Signal 2010; 13: 1341-58.
    • (2010) Antiox Redox Signal , vol.13 , pp. 1341-1358
    • Herrmann, J.M.1    Reimer, J.2
  • 48
    • 57649183232 scopus 로고    scopus 로고
    • The Redox Environment in the Mitochondrial Intermembrane Space is Maintained Separately from the Cytosol and Matrix
    • 29126-34
    • Hu J, Dong L, Outten CE. The Redox Environment in the Mitochondrial Intermembrane Space is Maintained Separately from the Cytosol and Matrix. J Biol Chem 2008; 29126-34.
    • (2008) J Biol Chem
    • Hu, J.1    Dong, L.2    Outten, C.E.3


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