메뉴 건너뛰기




Volumn 85, Issue , 2012, Pages 21-28

Electrochemical study of hydrogen peroxide formation in isolated mitochondria

Author keywords

Amperometry; Hydrogen peroxide; Mitochondria; Platinized carbon fiber microelectrodes

Indexed keywords

AMPEROMETRY; ATP SYNTHASE; ELECTROCHEMICAL ASSAYS; ELECTROCHEMICAL METHODOLOGY; ELECTROCHEMICAL STUDIES; MITOCHONDRIAL RESPIRATION; MOUSE LIVER; PATHOLOGICAL PROCESS; PEROXIDE FORMATIONS; PLATINIZED CARBON FIBER MICROELECTRODES; REACTIVE OXYGEN SPECIES; REACTIVE SPECIES; SIMULTANEOUS MEASUREMENT;

EID: 84857373542     PISSN: 15675394     EISSN: 1878562X     Source Type: Journal    
DOI: 10.1016/j.bioelechem.2011.11.005     Document Type: Article
Times cited : (21)

References (36)
  • 1
    • 23844558266 scopus 로고    scopus 로고
    • A mitochondrial paradigm of metabolic and degenerative diseases, aging, and cancer: a dawn for evolutionary medicine
    • Wallace D.C. A mitochondrial paradigm of metabolic and degenerative diseases, aging, and cancer: a dawn for evolutionary medicine. Annu. Rev. Genet. 2005, 39:359-407.
    • (2005) Annu. Rev. Genet. , vol.39 , pp. 359-407
    • Wallace, D.C.1
  • 4
    • 33646698671 scopus 로고    scopus 로고
    • Hydrogen peroxide: a signaling messenger
    • Stone J.R., Yang S. Hydrogen peroxide: a signaling messenger. Antioxid. Redox Signal. 2006, 8:243-270.
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 243-270
    • Stone, J.R.1    Yang, S.2
  • 5
    • 34548148201 scopus 로고    scopus 로고
    • Hydrogen peroxide: a metabolic by-product or a common mediator of ageing signal
    • Giorgio M., Trinei M., Migliaccio E., Pelicci P.G. Hydrogen peroxide: a metabolic by-product or a common mediator of ageing signal. Nat. Rev. Mol. Cell Biol. 2007, 8:722-728.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 722-728
    • Giorgio, M.1    Trinei, M.2    Migliaccio, E.3    Pelicci, P.G.4
  • 6
    • 67650248980 scopus 로고    scopus 로고
    • Oxygen sensitivity of mitochondrial reactive oxygen species generation depends on metabolic conditions
    • Hoffman D.L., Brookes P.S.J. Oxygen sensitivity of mitochondrial reactive oxygen species generation depends on metabolic conditions. Biol. Chem. 2009, 284:16236-16245.
    • (2009) Biol. Chem. , vol.284 , pp. 16236-16245
    • Hoffman, D.L.1    Brookes, P.S.J.2
  • 7
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • Murphy M.P. How mitochondria produce reactive oxygen species. Biochem. J. 2009, 417:1-13.
    • (2009) Biochem. J. , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 8
    • 33846225260 scopus 로고    scopus 로고
    • Response of mitochondrial reactive oxygen species generation to steady-state oxygen tension: implications for hypoxic cell signaling
    • Hoffman D.L., Salter J.D., Brookes P.S. Response of mitochondrial reactive oxygen species generation to steady-state oxygen tension: implications for hypoxic cell signaling. Am. J. Physiol. Heart Circ. Physiol. 2007, 292:H101-H108.
    • (2007) Am. J. Physiol. Heart Circ. Physiol. , vol.292
    • Hoffman, D.L.1    Salter, J.D.2    Brookes, P.S.3
  • 9
    • 34250745912 scopus 로고    scopus 로고
    • The Qo site of the mitochondrial complex III is required for the transduction of hypoxic signaling via reactive oxygen species production
    • Bell E.L., Klimova T.A., Eisenbart J., Moraes C.T., Murphy M.P., Budinger G.R., Chandel N.S. The Qo site of the mitochondrial complex III is required for the transduction of hypoxic signaling via reactive oxygen species production. Cell Biol. 2007, 177:1029-1036.
    • (2007) Cell Biol. , vol.177 , pp. 1029-1036
    • Bell, E.L.1    Klimova, T.A.2    Eisenbart, J.3    Moraes, C.T.4    Murphy, M.P.5    Budinger, G.R.6    Chandel, N.S.7
  • 10
    • 0035884737 scopus 로고    scopus 로고
    • Measurement of oxidative stress by EPR radical-probe technique
    • Valgimigli L., Pedulli G.F., Paolini M. Measurement of oxidative stress by EPR radical-probe technique. Free Radic. Biol. Med. 2001, 31:708-716.
    • (2001) Free Radic. Biol. Med. , vol.31 , pp. 708-716
    • Valgimigli, L.1    Pedulli, G.F.2    Paolini, M.3
  • 12
    • 5344234747 scopus 로고    scopus 로고
    • Detection of hydrogen peroxide with Amplex Red: interference by NADH and reduced glutathione auto-oxidation
    • Votyakova T.V., Reynolds I.J. Detection of hydrogen peroxide with Amplex Red: interference by NADH and reduced glutathione auto-oxidation. Arch. Biochem. Biophys. 2004, 431:138-144.
    • (2004) Arch. Biochem. Biophys. , vol.431 , pp. 138-144
    • Votyakova, T.V.1    Reynolds, I.J.2
  • 13
    • 29244444522 scopus 로고    scopus 로고
    • Fluorescence probes used for detection of reactive oxygen species
    • Gomes A., Fernandes E., Lima J.L.J. Fluorescence probes used for detection of reactive oxygen species. Biochem. Biophys. Methods 2005, 65:45-80.
    • (2005) Biochem. Biophys. Methods , vol.65 , pp. 45-80
    • Gomes, A.1    Fernandes, E.2    Lima, J.L.J.3
  • 14
    • 2942572700 scopus 로고    scopus 로고
    • Measuring reactive species and oxidative damage in vivo and in cell culture: how should you do it and what do the results mean?
    • Halliwell B., Whiteman M. Measuring reactive species and oxidative damage in vivo and in cell culture: how should you do it and what do the results mean?. Br. J. Pharmacol. 2004, 142:231-255.
    • (2004) Br. J. Pharmacol. , vol.142 , pp. 231-255
    • Halliwell, B.1    Whiteman, M.2
  • 15
    • 16544379743 scopus 로고    scopus 로고
    • Oxidative stress in cancer prone xeroderma pigmentosum fibroblasts, real-time and single cell monitoring of superoxide and nitric oxide production with microelectrodes
    • Arbault S., Sojic N., Bruce D., Amatore C., Sarasin A., Vuillaume M. Oxidative stress in cancer prone xeroderma pigmentosum fibroblasts, real-time and single cell monitoring of superoxide and nitric oxide production with microelectrodes. Carcinogenesis 2004, 25:509-515.
    • (2004) Carcinogenesis , vol.25 , pp. 509-515
    • Arbault, S.1    Sojic, N.2    Bruce, D.3    Amatore, C.4    Sarasin, A.5    Vuillaume, M.6
  • 16
    • 49249083962 scopus 로고    scopus 로고
    • Real-time amperometric analysis of reactive oxygen and nitrogen species released by single immunostimulated macrophages
    • Amatore C., Arbault S., Bouton C., Drapier J.C., Ghandour H., Koh A.C. Real-time amperometric analysis of reactive oxygen and nitrogen species released by single immunostimulated macrophages. ChemBioChem 2008, 9:1472-1480.
    • (2008) ChemBioChem , vol.9 , pp. 1472-1480
    • Amatore, C.1    Arbault, S.2    Bouton, C.3    Drapier, J.C.4    Ghandour, H.5    Koh, A.C.6
  • 17
    • 33645758212 scopus 로고    scopus 로고
    • Monitoring in real time with a microelectrode the release of reactive oxygen and nitrogen species by a single macrophage stimulated by its membrane mechanical depolarization
    • Amatore C., Arbault S., Bouton C., Coffi K., Drapier J.C., Ghandour H., Tong Y. Monitoring in real time with a microelectrode the release of reactive oxygen and nitrogen species by a single macrophage stimulated by its membrane mechanical depolarization. ChemBioChem 2006, 7:653-661.
    • (2006) ChemBioChem , vol.7 , pp. 653-661
    • Amatore, C.1    Arbault, S.2    Bouton, C.3    Coffi, K.4    Drapier, J.C.5    Ghandour, H.6    Tong, Y.7
  • 19
    • 0015592696 scopus 로고
    • The characteristics of the "peroxidatic" reaction of catalase in ethanol oxidation
    • Oshino N., Oshino R., Chance B. The characteristics of the "peroxidatic" reaction of catalase in ethanol oxidation. Biochem. J. 1973, 131:555-563.
    • (1973) Biochem. J. , vol.131 , pp. 555-563
    • Oshino, N.1    Oshino, R.2    Chance, B.3
  • 20
    • 0015038124 scopus 로고
    • Kinetics and mechanisms of catalase in peroxisomes of the mitochondrial fraction
    • Chance B., Oshino N. Kinetics and mechanisms of catalase in peroxisomes of the mitochondrial fraction. Biochem. J. 1971, 122:225-233.
    • (1971) Biochem. J. , vol.122 , pp. 225-233
    • Chance, B.1    Oshino, N.2
  • 21
    • 0025830348 scopus 로고
    • K+ conductance of the inner mitochondrial membrane. A study of the inducible uniport for monovalent cations
    • Nicolli A., Redetti A., Bernardi P., The P. K+ conductance of the inner mitochondrial membrane. A study of the inducible uniport for monovalent cations. J. Biol. Chem. 1991, 26:9465-9470.
    • (1991) J. Biol. Chem. , vol.26 , pp. 9465-9470
    • Nicolli, A.1    Redetti, A.2    Bernardi, P.3    The, P.4
  • 22
    • 0042433242 scopus 로고    scopus 로고
    • 2 production by membrane potential and NAD(P)H redox state
    • 2 production by membrane potential and NAD(P)H redox state. J. Neurochem. 2003, 86:1101-1107.
    • (2003) J. Neurochem. , vol.86 , pp. 1101-1107
    • Starkov, A.A.1    Fiskum, G.2
  • 23
    • 0030729851 scopus 로고    scopus 로고
    • Protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria
    • Korshunov S.S., Skulachev V.P., Starkov High A.A. Protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria. FEBS Lett. 1997, 416:15-18.
    • (1997) FEBS Lett. , vol.416 , pp. 15-18
    • Korshunov, S.S.1    Skulachev, V.P.2    Starkov High, A.A.3
  • 26
    • 64549096768 scopus 로고    scopus 로고
    • Reduction of hydrophilic ubiquinones by the flavin in mitochondrial NADH:ubiquinone oxidoreductase (Complex I) and production of reactive oxygen species
    • King M.S., Sharpley M.S., Hirst J. Reduction of hydrophilic ubiquinones by the flavin in mitochondrial NADH:ubiquinone oxidoreductase (Complex I) and production of reactive oxygen species. Biochemistry 2009, 48:2053-2062.
    • (2009) Biochemistry , vol.48 , pp. 2053-2062
    • King, M.S.1    Sharpley, M.S.2    Hirst, J.3
  • 27
    • 43049141441 scopus 로고    scopus 로고
    • Diphenyleneiodonium acutely inhibits reactive oxygen species production by mitochondrial complex I during reverse, but not forward electron transport
    • Lambert A.J., Buckingham J.A., Boysen H.M., Brand M.D. Diphenyleneiodonium acutely inhibits reactive oxygen species production by mitochondrial complex I during reverse, but not forward electron transport. Biochim. Biophys. Acta 2008, 1777:397-403.
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 397-403
    • Lambert, A.J.1    Buckingham, J.A.2    Boysen, H.M.3    Brand, M.D.4
  • 28
    • 0142150051 scopus 로고    scopus 로고
    • Mitochondrial formation of reactive oxygen species
    • Turrens J.F. Mitochondrial formation of reactive oxygen species. J. Physiol. 2003, 552:335-344.
    • (2003) J. Physiol. , vol.552 , pp. 335-344
    • Turrens, J.F.1
  • 29
    • 0035863011 scopus 로고    scopus 로고
    • Mitochondrial respiratory chain-dependent generation of superoxide anion and its release into the intermembrane space
    • Han D., Williams E., Cadenas E. Mitochondrial respiratory chain-dependent generation of superoxide anion and its release into the intermembrane space. Biochem. J. 2001, 353:411-416.
    • (2001) Biochem. J. , vol.353 , pp. 411-416
    • Han, D.1    Williams, E.2    Cadenas, E.3
  • 30
    • 46449087496 scopus 로고    scopus 로고
    • Fatty acids as modulators of the cellular production of reactive oxygen species
    • Schonfeld P., Wojtczak L. Fatty acids as modulators of the cellular production of reactive oxygen species. Free Radic. Biol. Med. 2008, 45:231-241.
    • (2008) Free Radic. Biol. Med. , vol.45 , pp. 231-241
    • Schonfeld, P.1    Wojtczak, L.2
  • 31
    • 2342431848 scopus 로고    scopus 로고
    • Opening of the mitochondrial permeability transition pore induces reactive oxygen species production at the level of the respiratory chain complex I
    • Batandier C., Leverve X., Fontaine E. Opening of the mitochondrial permeability transition pore induces reactive oxygen species production at the level of the respiratory chain complex I. J. Biol. Chem. 2004, 279:17197-17204.
    • (2004) J. Biol. Chem. , vol.279 , pp. 17197-17204
    • Batandier, C.1    Leverve, X.2    Fontaine, E.3
  • 32
    • 67349200007 scopus 로고    scopus 로고
    • Supramolecular organization of ATP synthase and respiratory chain in mitochondrial membranes
    • Wittig I., Schagger H. Supramolecular organization of ATP synthase and respiratory chain in mitochondrial membranes. Biochim. Biophys. Acta 2009, 1787:672-680.
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 672-680
    • Wittig, I.1    Schagger, H.2
  • 33
    • 77953357281 scopus 로고    scopus 로고
    • Ageing alters the supramolecular architecture of OxPhos complexes in rat brain cortex
    • Frenzel M., Rommelspacher H., Sugawa M.D., Dencher N.A. Ageing alters the supramolecular architecture of OxPhos complexes in rat brain cortex. Exp. Gerontol. 2010, 45:563-572.
    • (2010) Exp. Gerontol. , vol.45 , pp. 563-572
    • Frenzel, M.1    Rommelspacher, H.2    Sugawa, M.D.3    Dencher, N.A.4
  • 34
    • 33745684904 scopus 로고    scopus 로고
    • Mitochondrial ROS-induced ROS release: an update and review
    • Zorov D.B., Juhaszova M., Sollott S.J. Mitochondrial ROS-induced ROS release: an update and review. Biochim. Biophys. Acta 2006, 1757:509-517.
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 509-517
    • Zorov, D.B.1    Juhaszova, M.2    Sollott, S.J.3
  • 35
    • 0034518449 scopus 로고    scopus 로고
    • Mitochondria and Ca(2+)in cell physiology and pathophysiology
    • Duchen M.R. Mitochondria and Ca(2+)in cell physiology and pathophysiology. Cell Calcium 2000, 28:339-348.
    • (2000) Cell Calcium , vol.28 , pp. 339-348
    • Duchen, M.R.1
  • 36
    • 55949118714 scopus 로고    scopus 로고
    • Exercise-induced oxidative stress: cellular mechanisms and impact on muscle force production
    • Powers S.K., Jackson M.J. Exercise-induced oxidative stress: cellular mechanisms and impact on muscle force production. Physiol. Rev. 2008, 88:1243-1276.
    • (2008) Physiol. Rev. , vol.88 , pp. 1243-1276
    • Powers, S.K.1    Jackson, M.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.