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Volumn 585, Issue 2, 2011, Pages 385-389

Molecular identification of the enzyme responsible for the mitochondrial NADH-supported ammonium-dependent hydrogen peroxide production

Author keywords

Ammonium; Dihydrolipoyl dehydrogenase; Hydrogen peroxide; Mitochondria; Reactive oxygen species

Indexed keywords

AMMONIA; DIHYDROLIPOAMIDE DEHYDROGENASE; HYDROGEN PEROXIDE; PEPTIDE DERIVATIVE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; TRYPSIN;

EID: 78651366651     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.12.019     Document Type: Article
Times cited : (38)

References (27)
  • 1
    • 78651031094 scopus 로고
    • The respiratory chain and oxidative phosphorylation
    • B. Chance, and G.B. Williams The respiratory chain and oxidative phosphorylation Adv. Enzymol. 17 1956 65 134
    • (1956) Adv. Enzymol. , vol.17 , pp. 65-134
    • Chance, B.1    Williams, G.B.2
  • 2
    • 0015363173 scopus 로고
    • The cellular production of hydrogen peroxide
    • A. Boveris, N. Oshino, and B. Chance The cellular production of hydrogen peroxide Biochem. J. 128 1972 617 630
    • (1972) Biochem. J. , vol.128 , pp. 617-630
    • Boveris, A.1    Oshino, N.2    Chance, B.3
  • 3
    • 25444469412 scopus 로고    scopus 로고
    • Mitochondrial metabolism of reactive oxygen species
    • DOI 10.1007/s10541-005-0102-7
    • A.Yu. Andreev, Yu.E. Kushnareva, and A.A. Starkov Mitochondrial metabolism of reactive oxygen species Biochemistry (Moscow) 70 2005 200 214 (Pubitemid 40512329)
    • (2005) Biochemistry (Moscow) , vol.70 , Issue.2 , pp. 200-214
    • Andreyev, A.Yu.1    Kushnareva, Yu.E.2    Starkov, A.A.3
  • 4
    • 24144464489 scopus 로고    scopus 로고
    • Production of reactive oxygen species in brain mitochondria: Contribution by electron transport chain and non-electron transport chain sources
    • DOI 10.1089/ars.2005.7.1140
    • V. Adam-Vizi Production of reactive oxygen species in brain mitochondria: contribution by electron transport chain and non-electron transport chain sources Antioxid. Redox Signal. 7 2005 1140 1149 (Pubitemid 41232509)
    • (2005) Antioxidants and Redox Signaling , vol.7 , Issue.9-10 , pp. 1140-1149
    • Adam-Vizi, V.1
  • 5
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • M.P. Murphy How mitochondria produce reactive oxygen species Biochem. J. 417 2009 1 13
    • (2009) Biochem. J. , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 6
    • 0014217470 scopus 로고
    • Partial resolution of the enzymes catalyzing oxidative phosphorylation. XV. Reverse electron transfer in the flavin-cytochrome b region of the respiratory chain of beef heart submitochondrial particles
    • P.C. Hinkle, R.A. Butow, E. Racker, and B. Chance Partial resolution of the enzymes catalyzing oxidative phosphorylation. XV. Reverse electron transfer in the flavin-cytochrome b region of the respiratory chain of beef heart submitochondrial particles J. Biol. Chem. 242 1967 5169 5173
    • (1967) J. Biol. Chem. , vol.242 , pp. 5169-5173
    • Hinkle, P.C.1    Butow, R.A.2    Racker, E.3    Chance, B.4
  • 7
    • 0018393931 scopus 로고
    • NADH- and NADPH-dependent formation of superoxide anions by bovine heart submitochondrial particles and NADH-ubiquinone reductase preparation
    • K. Takeshige, and S. Minakami NADH- and NADPH-dependent formation of superoxide anions by bovine heart submitochondrial particles and NADH-ubiquinone reductase preparation Biochem. J. 180 1979 129 135 (Pubitemid 9172746)
    • (1979) Biochemical Journal , vol.180 , Issue.1 , pp. 129-135
    • Takeshige, K.1    Minakami, S.2
  • 8
    • 0024297325 scopus 로고
    • Studies on the electron transfer pathway, topography of iron-sulfur centers, and site of coupling in NADH-Q oxidoreductase
    • A.I.G. Krishnamoorthy, and P. Hinkle Studies on the electron transfer pathway, topography of iron-sulfur centers, and site of coupling in NADH-Q oxidoreductase J. Biol. Chem. 263 1988 17566 17575
    • (1988) J. Biol. Chem. , vol.263 , pp. 17566-17575
    • Krishnamoorthy, A.I.G.1    Hinkle, P.2
  • 9
    • 0020586897 scopus 로고
    • Effect of electron transfer inhibitors on superoxide generation in the cytochrome bc1 site of the mitochondrial respiratory chain
    • M.Yu. Ksenzenko, A.A. Konstantinov, G.B. Khomutov, A.N. Tikhonov, and E.K. Ruuge Effect of electron transfer inhibitors on superoxide generation in the cytochrome bc1 site of the mitochondrial respiratory chain FEBS Lett. 155 1983 19 24
    • (1983) FEBS Lett. , vol.155 , pp. 19-24
    • Ksenzenko, M.Yu.1    Konstantinov, A.A.2    Khomutov, G.B.3    Tikhonov, A.N.4    Ruuge, E.K.5
  • 10
    • 0141815741 scopus 로고    scopus 로고
    • Production of reactive oxygen species by mitochondria: Central role of complex III
    • DOI 10.1074/jbc.M304854200
    • Q. Chen, E.J. Vazquez, S. Moghaddas, C.L. Hoppel, and E.J. Lesnefsky Production of reactive oxygen species by mitochondria. Central role of complex III J. Biol. Chem. 278 2003 36027 36031 (Pubitemid 37139922)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.38 , pp. 36027-36031
    • Chen, Q.1    Vazquez, E.J.2    Moghaddas, S.3    Hoppel, C.L.4    Lesnefsky, E.J.5
  • 12
    • 0016148483 scopus 로고
    • Superoxide radicals as precursors of mitochondrial hydrogen peroxide
    • G. Loschen, A. Azzi, C. Richter, and L. Flohé Superoxide radicals as precursors of mitochondrial hydrogen peroxide FEBS Lett. 42 1974 68 72
    • (1974) FEBS Lett. , vol.42 , pp. 68-72
    • Loschen, G.1    Azzi, A.2    Richter, C.3    Flohé, L.4
  • 13
    • 33745628757 scopus 로고    scopus 로고
    • Generation of superoxide by the mitochondrial Complex i
    • V.G. Grivennikova, and A.D. Vinogradov Generation of superoxide by the mitochondrial Complex I Biochim. Biophys. Acta 1757 2006 553 561
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 553-561
    • Grivennikova, V.G.1    Vinogradov, A.D.2
  • 14
    • 47849099861 scopus 로고    scopus 로고
    • Ammonium-dependent hydrogen peroxide production by mitochondria
    • V.G. Grivennikova, G. Cecchini, and A.D. Vinogradov Ammonium-dependent hydrogen peroxide production by mitochondria FEBS Lett. 582 2008 2719 2724
    • (2008) FEBS Lett. , vol.582 , pp. 2719-2724
    • Grivennikova, V.G.1    Cecchini, G.2    Vinogradov, A.D.3
  • 15
    • 77953809952 scopus 로고    scopus 로고
    • What are the sources of hydrogen peroxide production by heart mitochondria?
    • V.G. Grivennikova, A.V. Kareyeva, and A.D. Vinogradov What are the sources of hydrogen peroxide production by heart mitochondria? Biochim. Biophys. Acta 1797 2010 939 944
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 939-944
    • Grivennikova, V.G.1    Kareyeva, A.V.2    Vinogradov, A.D.3
  • 16
    • 0001693872 scopus 로고
    • Studies on the electron transfer system. IV. The electron transfer particles
    • F.L. Crane, J.L. Glenn, and D. Green Studies on the electron transfer system. IV. The electron transfer particles Biochem. Biophys. Acta 22 1956 475 487
    • (1956) Biochem. Biophys. Acta , vol.22 , pp. 475-487
    • Crane, F.L.1    Glenn, J.L.2    Green, D.3
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0031573401 scopus 로고    scopus 로고
    • A stable nonfluorescent derivative of resorufin for the fluorometric determination of trace hydrogen peroxide: Applications in detecting the activity of phagocyte NADPH oxidase and other oxidases
    • DOI 10.1006/abio.1997.2391
    • M. Zhou, Z. Diwu, N. Panchuk-Voloshina, and R.P. Haugland A stable nonfluorescent derivative of resorufin for the fluorometric determination of trace hydrogen peroxide: applications in detecting the activity of phagocyte NADPH oxidase and other oxidases Anal. Biochem. 253 1997 162 168 (Pubitemid 27508167)
    • (1997) Analytical Biochemistry , vol.253 , Issue.2 , pp. 162-168
    • Zhou, M.1    Diwu, Z.2    Panchuk-Voloshina, N.3    Haugland, R.P.4
  • 19
    • 0037328645 scopus 로고    scopus 로고
    • In situ assay of the intramitochondrial enzymes: Use of alamethicin for permeabilization of mitochondria
    • I.S. Gostimskaya, V.G. Grivennikova, T.V. Zharova, L.E. Bakeeva, and A.D. Vinogradov In situ assay of the intramitochondrial enzymes: use of alamethicin for permeabilization of mitochondria Anal. Biochem. 313 2003 46 52
    • (2003) Anal. Biochem. , vol.313 , pp. 46-52
    • Gostimskaya, I.S.1    Grivennikova, V.G.2    Zharova, T.V.3    Bakeeva, L.E.4    Vinogradov, A.D.5
  • 20
    • 34648816537 scopus 로고    scopus 로고
    • Redox-dependent change of nucleotide affinity to the active site of the mammalian complex I
    • DOI 10.1021/bi7009822
    • V.G. Grivennikova, A.B. Kotlyar, J.S. Karliner, G. Cecchini, and A.D. Vinogradov Redox-dependent change of nucleotide affinity to the active site of the mammalian complex I Biochemistry 46 2007 10971 10978 (Pubitemid 47463048)
    • (2007) Biochemistry , vol.46 , Issue.38 , pp. 10971-10978
    • Grivennikova, V.G.1    Kotlyar, A.B.2    Karliner, J.S.3    Cecchini, G.4    Vinogradov, A.D.5
  • 21
    • 2942557132 scopus 로고    scopus 로고
    • Dihydrolipoamide dehydrogenase from porcine heart catalyzes NADH-dependent scavenging of nitric oxide
    • DOI 10.1016/j.febslet.2004.05.024, PII S0014579304006374
    • A.U. Igamberdiev, N.V. Bykova, W. Ens, and R.D. Hill Dihydrolipoamide dehydrogenase from porcine heart catalyzes NADH-dependent scavenging of nitric oxide FEBS Lett. 568 2004 146 150 (Pubitemid 38757971)
    • (2004) FEBS Letters , vol.568 , Issue.1-3 , pp. 146-150
    • Igamberdiev, A.U.1    Bykova, N.V.2    Ens, W.3    Hill, R.D.4
  • 22
    • 0032991061 scopus 로고    scopus 로고
    • Ubiquinone is reduced by lipoamide dehydrogenase and this reaction is potently stimulated by zinc
    • DOI 10.1016/S0014-5793(99)00363-4, PII S0014579399003634
    • J.M. Olsson, L. Xia, L.C. Eriksson, and M. Björnstedt Ubiquinone is reduced by lipoamide dehydrogenase and this reaction is potently stimulated by zinc FEBS Lett. 448 1999 190 192 (Pubitemid 29151658)
    • (1999) FEBS Letters , vol.448 , Issue.1 , pp. 190-192
    • Olsson, J.M.1    Xia, L.2    Eriksson, L.C.3    Bjornstedt, M.4
  • 23
    • 0037102005 scopus 로고    scopus 로고
    • Lipoyl dehydrogenase catalyzes reduction of nitrated DNA and protein adducts using dihydrolipoic acid or ubiquinol as the cofactor
    • H.-J.C. Chen, Y.-M. Chen, and C.-M. Chang Lipoyl dehydrogenase catalyzes reduction of nitrated DNA and protein adducts using dihydrolipoic acid or ubiquinol as the cofactor Chem. Biol. Interact. 140 2002 199 213
    • (2002) Chem. Biol. Interact. , vol.140 , pp. 199-213
    • Chen, H.-J.C.1    Chen, Y.-M.2    Chang, C.-M.3
  • 25
    • 46349103431 scopus 로고    scopus 로고
    • + interaction with NADH: Ubiquinone oxidoreductase (complex I)
    • + interaction with NADH: Ubiquinone oxidoreductase (complex I) Biochim. Biophys. Acta 1777 2008 729 734
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 729-734
    • Vinogradov, A.D.1
  • 26
    • 0000198395 scopus 로고
    • Concentrations of metabolites in animal tissues
    • D.H. Williamson, and J.T. Brosnan Concentrations of metabolites in animal tissues H.U. Bergmeyer, K. Gawehn, Methods of Enzymatic Analysis 1974 Verlag Chemie Weinhem, Academic Press, Inc. NY and London 2266 2301
    • (1974) Methods of Enzymatic Analysis , pp. 2266-2301
    • Williamson, D.H.1    Brosnan, J.T.2
  • 27
    • 65849236255 scopus 로고    scopus 로고
    • The mitochondrial pool of free amino acids reflects the composition of mitochondrial DNA-encoded proteins: Indication of a post-translation quality control for protein synthesis
    • C. Ross-Inta, C.-Y. Tsai, and C. Giulivi The mitochondrial pool of free amino acids reflects the composition of mitochondrial DNA-encoded proteins: indication of a post-translation quality control for protein synthesis Biosci. Rep. 28 2008 239 249
    • (2008) Biosci. Rep. , vol.28 , pp. 239-249
    • Ross-Inta, C.1    Tsai, C.-Y.2    Giulivi, C.3


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