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Volumn 607, Issue , 2016, Pages 8-19

Mitochondrial nitric oxide production supported by reverse electron transfer

Author keywords

Complex I; Inside out particles; Mitochondrial nitric oxide synthase; Nitric oxide; Reverse electron transfer

Indexed keywords

ADENOSINE TRIPHOSPHATE; ENZYME ANTIBODY; MITOCHONDRIAL NITRIC OXIDE SYNTHASE; NEURONAL NITRIC OXIDE SYNTHASE; NITRIC OXIDE; NITRIC OXIDE SYNTHASE; RECOMBINANT ENZYME; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; ROTENONE; SUCCINIC ACID; UNCLASSIFIED DRUG; ALCOHOL DEHYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; RECOMBINANT PROTEIN;

EID: 84982193810     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2016.08.010     Document Type: Article
Times cited : (21)

References (69)
  • 1
    • 0030697859 scopus 로고    scopus 로고
    • Nitric oxide synthase activity in mitochondria
    • [1] Ghafourifar, P., Richter, C., Nitric oxide synthase activity in mitochondria. FEBS Lett. 418 (1997), 291–296 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9428730.
    • (1997) FEBS Lett. , vol.418 , pp. 291-296
    • Ghafourifar, P.1    Richter, C.2
  • 2
    • 0032079478 scopus 로고    scopus 로고
    • Production of nitric oxide by mitochondria
    • [2] Giulivi, C., Poderoso, J.J., Boveris, A., Production of nitric oxide by mitochondria. J. Biol. Chem. 273 (1998), 11038–11043 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9556586.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11038-11043
    • Giulivi, C.1    Poderoso, J.J.2    Boveris, A.3
  • 3
    • 0037064058 scopus 로고    scopus 로고
    • Biochemistry of mitochondrial nitric-oxide synthase
    • [3] Elfering, S.L., Sarkela, T.M., Giulivi, C., Biochemistry of mitochondrial nitric-oxide synthase. J. Biol. Chem. 277 (2002), 38079–38086 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12154090.
    • (2002) J. Biol. Chem. , vol.277 , pp. 38079-38086
    • Elfering, S.L.1    Sarkela, T.M.2    Giulivi, C.3
  • 4
    • 0035923615 scopus 로고    scopus 로고
    • Identification of a neuronal nitric oxide synthase in isolated cardiac mitochondria using electrochemical detection
    • [4] Kanai, A.J., Pearce, L.L., Clemens, P.R., Birder, L.A., VanBibber, M.M., Choi, S.Y., et al. Identification of a neuronal nitric oxide synthase in isolated cardiac mitochondria using electrochemical detection. Proc. Natl. Acad. Sci. U. S. A. 98 (2001), 14126–14131, 10.1073/pnas.241380298.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 14126-14131
    • Kanai, A.J.1    Pearce, L.L.2    Clemens, P.R.3    Birder, L.A.4    VanBibber, M.M.5    Choi, S.Y.6
  • 5
    • 0036439030 scopus 로고    scopus 로고
    • Pharmacological regulation of mitochondrial nitric oxide synthase
    • [5] Boveris, A., Arnaiz, S.L., Bustamante, J., Alvarez, S., Valdez, L., Boveris, A.D., et al. Pharmacological regulation of mitochondrial nitric oxide synthase. Methods Enzym. 359 (2002), 328–339 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12481584.
    • (2002) Methods Enzym. , vol.359 , pp. 328-339
    • Boveris, A.1    Arnaiz, S.L.2    Bustamante, J.3    Alvarez, S.4    Valdez, L.5    Boveris, A.D.6
  • 6
    • 66949149495 scopus 로고    scopus 로고
    • Mitochondrial nitric oxide metabolism during rat heart adaptation to high altitude: effect of sildenafil, L-NAME, and L-arginine treatments
    • [6] Zaobornyj, T., Valdez, L.B., Iglesias, D.E., Gasco, M., Gonzales, G.F., Boveris, A., Mitochondrial nitric oxide metabolism during rat heart adaptation to high altitude: effect of sildenafil, L-NAME, and L-arginine treatments. Am. J. Physiol. Hear. Circ. Physiol. 296 (2009), H1741–H1747 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=19346458.
    • (2009) Am. J. Physiol. Hear. Circ. Physiol. , vol.296 , pp. H1741-H1747
    • Zaobornyj, T.1    Valdez, L.B.2    Iglesias, D.E.3    Gasco, M.4    Gonzales, G.F.5    Boveris, A.6
  • 7
    • 33646118481 scopus 로고    scopus 로고
    • Mitochondrial metabolic states and membrane potential modulate mtNOS activity
    • [7] Valdez, L.B., Zaobornyj, T., Boveris, A., Mitochondrial metabolic states and membrane potential modulate mtNOS activity. Biochim. Biophys. Acta 1757 (2006), 166–172 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16624252.
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 166-172
    • Valdez, L.B.1    Zaobornyj, T.2    Boveris, A.3
  • 8
    • 34249819641 scopus 로고    scopus 로고
    • Mitochondrial nitric oxide synthase, a voltage-dependent enzyme, is responsible for nitric oxide diffusion to cytosol
    • [8] Valdez, L.B., Boveris, A., Mitochondrial nitric oxide synthase, a voltage-dependent enzyme, is responsible for nitric oxide diffusion to cytosol. Front. Biosci. 12 (2007), 1210–1219 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=17127374.
    • (2007) Front. Biosci. , vol.12 , pp. 1210-1219
    • Valdez, L.B.1    Boveris, A.2
  • 9
    • 46149115394 scopus 로고    scopus 로고
    • Control of muscle mitochondria by insulin entails activation of Akt2-mtNOS pathway: imlpications for the metabolic syndrome
    • [9] Finocchietto, P., Barreyro, F., Holod, S., Peralta, J., Franco, M.C., Méndez, C., et al. Control of muscle mitochondria by insulin entails activation of Akt2-mtNOS pathway: imlpications for the metabolic syndrome. PLoS One, 3, 2008, 10.1371/journal.pone.0001749.
    • (2008) PLoS One , vol.3
    • Finocchietto, P.1    Barreyro, F.2    Holod, S.3    Peralta, J.4    Franco, M.C.5    Méndez, C.6
  • 10
    • 33745609228 scopus 로고    scopus 로고
    • Mitochondrial metabolic states regulate nitric oxide and hydrogen peroxide diffusion to the cytosol
    • [10] Boveris, A., Valdez, L.B., Zaobornyj, T., Bustamante, J., Mitochondrial metabolic states regulate nitric oxide and hydrogen peroxide diffusion to the cytosol. Biochim. Biophys. Acta 1757 (2006), 535–542 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16615992.
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 535-542
    • Boveris, A.1    Valdez, L.B.2    Zaobornyj, T.3    Bustamante, J.4
  • 11
    • 28044464985 scopus 로고
    • Reversible inhibition of cytochrome c oxidase, the terminal enzyme of the mitochondrial respiratory chain, by nitric oxide. Implications for neurodegenerative diseases
    • [11] Cleeter, M.W., Cooper, J.M., Darley-Usmar, V.M., Moncada, S., Schapira, A.H., Reversible inhibition of cytochrome c oxidase, the terminal enzyme of the mitochondrial respiratory chain, by nitric oxide. Implications for neurodegenerative diseases. FEBS Lett. 345 (1994), 50–54 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8194600.
    • (1994) FEBS Lett. , vol.345 , pp. 50-54
    • Cleeter, M.W.1    Cooper, J.M.2    Darley-Usmar, V.M.3    Moncada, S.4    Schapira, A.H.5
  • 12
    • 10044230387 scopus 로고    scopus 로고
    • On the mechanism and biology of cytochrome oxidase inhibition by nitric oxide
    • [12] Antunes, F., Boveris, A., Cadenas, E., On the mechanism and biology of cytochrome oxidase inhibition by nitric oxide. Proc. Natl. Acad. Sci. U. S. A. 101 (2004), 16774–16779 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15546991.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 16774-16779
    • Antunes, F.1    Boveris, A.2    Cadenas, E.3
  • 13
    • 34648843079 scopus 로고    scopus 로고
    • On the biologic role of the reaction of NO with oxidized cytochrome c oxidase
    • [13] Antunes, F., Boveris, A., Cadenas, E., On the biologic role of the reaction of NO with oxidized cytochrome c oxidase. Antioxid. Redox Signal 9 (2007), 1569–1579 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=17665969.
    • (2007) Antioxid. Redox Signal , vol.9 , pp. 1569-1579
    • Antunes, F.1    Boveris, A.2    Cadenas, E.3
  • 14
    • 0029986691 scopus 로고    scopus 로고
    • Nitric oxide inhibits electron transfer and increases superoxide radical production in rat heart mitochondria and submitochondrial particles
    • [14] Poderoso, J.J., Carreras, M.C., Lisdero, C., Riobo, N., Schopfer, F., Boveris, A., Nitric oxide inhibits electron transfer and increases superoxide radical production in rat heart mitochondria and submitochondrial particles. Arch. Biochem. Biophys. 328 (1996), 85–92 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=8638942.
    • (1996) Arch. Biochem. Biophys. , vol.328 , pp. 85-92
    • Poderoso, J.J.1    Carreras, M.C.2    Lisdero, C.3    Riobo, N.4    Schopfer, F.5    Boveris, A.6
  • 15
    • 0034082985 scopus 로고    scopus 로고
    • Regulation of mitochondrial respiration by oxygen and nitric oxide
    • [15] Boveris, A., Costa, L.E., Poderoso, J.J., Carreras, M.C., Cadenas, E., Regulation of mitochondrial respiration by oxygen and nitric oxide. Ann. N. Y. Acad. Sci. 899 (2000), 121–135 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10863534.
    • (2000) Ann. N. Y. Acad. Sci. , vol.899 , pp. 121-135
    • Boveris, A.1    Costa, L.E.2    Poderoso, J.J.3    Carreras, M.C.4    Cadenas, E.5
  • 16
    • 84944184747 scopus 로고    scopus 로고
    • Nitric oxide interacts with mitochondrial complex III producing antimycin-like effects
    • [16] Iglesias, D.E., Bombicino, S.S., Valdez, L.B., Boveris, A., Nitric oxide interacts with mitochondrial complex III producing antimycin-like effects. Free Rad. Biol. Med. 89 (2015), 602–613, 10.1016/j.freeradbiomed.2015.08.024.
    • (2015) Free Rad. Biol. Med. , vol.89 , pp. 602-613
    • Iglesias, D.E.1    Bombicino, S.S.2    Valdez, L.B.3    Boveris, A.4
  • 17
    • 0033805760 scopus 로고    scopus 로고
    • Reactions of peroxynitrite in the mitochondrial matrix
    • [17] Valdez, L.B., Alvarez, S., Arnaiz, S.L., Schopfer, F., Carreras, M.C., Poderoso, J.J., et al. Reactions of peroxynitrite in the mitochondrial matrix. Free Radic. Biol. Med. 29 (2000), 349–356 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=11035264.
    • (2000) Free Radic. Biol. Med. , vol.29 , pp. 349-356
    • Valdez, L.B.1    Alvarez, S.2    Arnaiz, S.L.3    Schopfer, F.4    Carreras, M.C.5    Poderoso, J.J.6
  • 18
    • 37549027704 scopus 로고    scopus 로고
    • Association of mitochondrial nitric oxide synthase activity with respiratory chain complex I
    • [18] Parihar, M.S., Nazarewicz, R.R., Kincaid, E., Bringold, U., Ghafourifar, P., Association of mitochondrial nitric oxide synthase activity with respiratory chain complex I. Biochem. Biophys. Res. Commun. 366 (2008), 23–28 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=18036554.
    • (2008) Biochem. Biophys. Res. Commun. , vol.366 , pp. 23-28
    • Parihar, M.S.1    Nazarewicz, R.R.2    Kincaid, E.3    Bringold, U.4    Ghafourifar, P.5
  • 19
    • 33646186367 scopus 로고    scopus 로고
    • Hypothyroid phenotype is contributed by mitochondrial complex I inactivation due to translocated neuronal nitric-oxide synthase
    • [19] Franco, M.C., Antico Arciuch, V.G., Peralta, J.G., Galli, S., Levisman, D., Lopez, L.M., et al. Hypothyroid phenotype is contributed by mitochondrial complex I inactivation due to translocated neuronal nitric-oxide synthase. J. Biol. Chem. 281 (2006), 4779–4786 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16361261.
    • (2006) J. Biol. Chem. , vol.281 , pp. 4779-4786
    • Franco, M.C.1    Antico Arciuch, V.G.2    Peralta, J.G.3    Galli, S.4    Levisman, D.5    Lopez, L.M.6
  • 20
    • 33744951975 scopus 로고    scopus 로고
    • Architecture of active mammalian respiratory chain supercomplexes
    • [20] Schafer, E., Seelert, H., Reifschneider, N.H., Krause, F., Dencher, N.A., Vonck, J., Architecture of active mammalian respiratory chain supercomplexes. J. Biol. Chem. 281 (2006), 15370–15375 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16551638.
    • (2006) J. Biol. Chem. , vol.281 , pp. 15370-15375
    • Schafer, E.1    Seelert, H.2    Reifschneider, N.H.3    Krause, F.4    Dencher, N.A.5    Vonck, J.6
  • 21
    • 84896690861 scopus 로고    scopus 로고
    • Functional role of mitochondrial respiratory supercomplexes
    • [21] Genova, M.L., Lenaz, G., Functional role of mitochondrial respiratory supercomplexes. Biochim. Biophys. Acta 1837 (2014), 427–443 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=24246637.
    • (2014) Biochim. Biophys. Acta , vol.1837 , pp. 427-443
    • Genova, M.L.1    Lenaz, G.2
  • 22
    • 1042278126 scopus 로고    scopus 로고
    • Assembly of respiratory complexes I, III, and IV into NADH oxidase supercomplex stabilizes complex I in Paracoccus denitrificans
    • [22] Stroh, A., Anderka, O., Pfeiffer, K., Yagi, T., Finel, M., Ludwig, B., et al. Assembly of respiratory complexes I, III, and IV into NADH oxidase supercomplex stabilizes complex I in Paracoccus denitrificans. J. Biol. Chem. 279 (2004), 5000–5007 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=14610094.
    • (2004) J. Biol. Chem. , vol.279 , pp. 5000-5007
    • Stroh, A.1    Anderka, O.2    Pfeiffer, K.3    Yagi, T.4    Finel, M.5    Ludwig, B.6
  • 23
    • 20644435792 scopus 로고    scopus 로고
    • Mitochondrial type I nitric oxide synthase physically interacts with cytochrome c oxidase
    • [23] Persichini, T., Mazzone, V., Polticelli, F., Moreno, S., Venturini, G., Clementi, E., et al. Mitochondrial type I nitric oxide synthase physically interacts with cytochrome c oxidase. Neurosci. Lett. 384 (2005), 254–259 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15923083.
    • (2005) Neurosci. Lett. , vol.384 , pp. 254-259
    • Persichini, T.1    Mazzone, V.2    Polticelli, F.3    Moreno, S.4    Venturini, G.5    Clementi, E.6
  • 24
    • 0027104114 scopus 로고
    • The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains
    • [24] Walker, J.E., The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains. Q. Rev. Biophys. 25 (1992), 253–324 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1470679.
    • (1992) Q. Rev. Biophys. , vol.25 , pp. 253-324
    • Walker, J.E.1
  • 25
    • 0026487290 scopus 로고
    • Sequences of 20 subunits of NADH:ubiquinone oxidoreductase from bovine heart mitochondria. Application of a novel strategy for sequencing proteins using the polymerase chain reaction
    • [25] Walker, J.E., Arizmendi, J.M., Dupuis, A., Fearnley, I.M., Finel, M., Medd, S.M., et al. Sequences of 20 subunits of NADH:ubiquinone oxidoreductase from bovine heart mitochondria. Application of a novel strategy for sequencing proteins using the polymerase chain reaction. J. Mol. Biol. 226 (1992), 1051–1072 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=1518044.
    • (1992) J. Mol. Biol. , vol.226 , pp. 1051-1072
    • Walker, J.E.1    Arizmendi, J.M.2    Dupuis, A.3    Fearnley, I.M.4    Finel, M.5    Medd, S.M.6
  • 26
    • 0242555474 scopus 로고
    • The interaction of energy and electron transfer reactions in mitochondria. VI. The efficiency of the reaction
    • [26] Chance, B., Hollunger, G., The interaction of energy and electron transfer reactions in mitochondria. VI. The efficiency of the reaction. J. Biol. Chem. 236 (1961), 1577–1584 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=13692280.
    • (1961) J. Biol. Chem. , vol.236 , pp. 1577-1584
    • Chance, B.1    Hollunger, G.2
  • 27
    • 0001297030 scopus 로고
    • Endogenous ADP of mitochondria, an early phosphate acceptor of oxidative phosphorylation as disclosed by kinetic studies with C14 labelled ADP and ATP and with atractyloside
    • [27] Heldt, H.W., Jacobs, H., Klingenberg, M., Endogenous ADP of mitochondria, an early phosphate acceptor of oxidative phosphorylation as disclosed by kinetic studies with C14 labelled ADP and ATP and with atractyloside. Biochem. Biophys. Res. Commun. 18 (1965), 174–179 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=14282014.
    • (1965) Biochem. Biophys. Res. Commun. , vol.18 , pp. 174-179
    • Heldt, H.W.1    Jacobs, H.2    Klingenberg, M.3
  • 28
    • 0032490104 scopus 로고    scopus 로고
    • Catalytic properties of the mitochondrial NADH-ubiquinone oxidoreductase (Complex I) and the pseudo-reversible active/inactive enzyme transition
    • [28] Vinogradov, A.D., Catalytic properties of the mitochondrial NADH-ubiquinone oxidoreductase (Complex I) and the pseudo-reversible active/inactive enzyme transition. Biochim. Biophys. Acta - Bioenerg. 1364 (1998), 169–185, 10.1016/S0005-2728(98)00026-7.
    • (1998) Biochim. Biophys. Acta - Bioenerg. , vol.1364 , pp. 169-185
    • Vinogradov, A.D.1
  • 29
    • 0016045905 scopus 로고
    • Equilibrium relations between the oxidation-reduction reactions and the adenosine triphosphate synthesis in suspensions of isolated liver cells
    • [29] Wilson, D.F., Stubbs, M., Veech, R.L., Erecinska, M., Krebs, H.A., Equilibrium relations between the oxidation-reduction reactions and the adenosine triphosphate synthesis in suspensions of isolated liver cells. Biochem. J. 140 (1974), 57–64.
    • (1974) Biochem. J. , vol.140 , pp. 57-64
    • Wilson, D.F.1    Stubbs, M.2    Veech, R.L.3    Erecinska, M.4    Krebs, H.A.5
  • 30
    • 79955977892 scopus 로고    scopus 로고
    • Superoxide is produced by the reduced flavin in mitochondrial complex I: a single, unified mechanism that applies during both forward and reverse electron transfer
    • [30] Pryde, K.R., Hirst, J., Superoxide is produced by the reduced flavin in mitochondrial complex I: a single, unified mechanism that applies during both forward and reverse electron transfer. J. Biol. Chem. 286 (2011), 18056–18065 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=21393237.
    • (2011) J. Biol. Chem. , vol.286 , pp. 18056-18065
    • Pryde, K.R.1    Hirst, J.2
  • 31
    • 0032526039 scopus 로고    scopus 로고
    • Functional implications of nitric oxide produced by mitochondria in mitochondrial metabolism
    • [31] Giulivi, C., Functional implications of nitric oxide produced by mitochondria in mitochondrial metabolism. Biochem. J. 332:Pt 3 (1998), 673–679 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9620869.
    • (1998) Biochem. J. , vol.332 , pp. 673-679
    • Giulivi, C.1
  • 32
    • 0032079851 scopus 로고    scopus 로고
    • Purification and characterization of a nitric-oxide synthase from rat liver mitochondria
    • [32] Tatoyan, A., Giulivi, C., Purification and characterization of a nitric-oxide synthase from rat liver mitochondria. J. Biol. Chem. 273 (1998), 11044–11048 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9556587.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11044-11048
    • Tatoyan, A.1    Giulivi, C.2
  • 33
    • 0002312641 scopus 로고
    • The large-scale preparation and properties of heart mitochondria from slaughterhouse material
    • [33] Blair, P.V., The large-scale preparation and properties of heart mitochondria from slaughterhouse material. Methods Enzym. X (1967), 78–81.
    • (1967) Methods Enzym. , vol.10 , pp. 78-81
    • Blair, P.V.1
  • 34
    • 0017406503 scopus 로고
    • Production of superoxide radicals and hydrogen peroxide by NADH-ubiquinone reductase and ubiquinol-cytochrome c reductase from beef-heart mitochondria
    • [34] Cadenas, E., Boveris, A., Ragan, C.I., Stoppani, A.O., Production of superoxide radicals and hydrogen peroxide by NADH-ubiquinone reductase and ubiquinol-cytochrome c reductase from beef-heart mitochondria. Arch. Biochem. Biophys. 180 (1977), 248–257 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=195520.
    • (1977) Arch. Biochem. Biophys. , vol.180 , pp. 248-257
    • Cadenas, E.1    Boveris, A.2    Ragan, C.I.3    Stoppani, A.O.4
  • 35
    • 0017154414 scopus 로고
    • Role of ubiquinone in the mitochondrial generation of hydrogen peroxide
    • [35] Boveris, A., Cadenas, E., Stoppani, A.O., Role of ubiquinone in the mitochondrial generation of hydrogen peroxide. Biochem. J. 156 (1976), 435–444 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=182149.
    • (1976) Biochem. J. , vol.156 , pp. 435-444
    • Boveris, A.1    Cadenas, E.2    Stoppani, A.O.3
  • 36
    • 77956996049 scopus 로고
    • The preparation and properties of DNPH-cytochrome c reductase (complex I-III of the respiratory chain)
    • [36] Hatefi, Y., Rieske, J.S., The preparation and properties of DNPH-cytochrome c reductase (complex I-III of the respiratory chain). Methods Enzym. X (1967), 225–231.
    • (1967) Methods Enzym. , vol.10 , pp. 225-231
    • Hatefi, Y.1    Rieske, J.S.2
  • 37
    • 0019083215 scopus 로고
    • Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria
    • [37] Turrens, J.F., Boveris, A., Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria. Biochem. J. 191 (1980), 421–427 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=6263247.
    • (1980) Biochem. J. , vol.191 , pp. 421-427
    • Turrens, J.F.1    Boveris, A.2
  • 38
    • 0018401677 scopus 로고
    • Isolation of mitochondria with emphasis on heart mitochondria from small amounts of tissue
    • [38] Mela, I., Seitz, S., Isolation of mitochondria with emphasis on heart mitochondria from small amounts of tissue. Meth. Enzymol. 55 (1979), 39–46.
    • (1979) Meth. Enzymol. , vol.55 , pp. 39-46
    • Mela, I.1    Seitz, S.2
  • 39
    • 0031740358 scopus 로고    scopus 로고
    • Regulation of mitochondrial respiration by adenosine diphosphate, oxygen, and nitric oxide
    • [39] Boveris, A., Costa, L.E., Cadenas, E., Poderoso, J.J., Regulation of mitochondrial respiration by adenosine diphosphate, oxygen, and nitric oxide. Methods Enzym. 301 (1999), 188–198 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9919567.
    • (1999) Methods Enzym. , vol.301 , pp. 188-198
    • Boveris, A.1    Costa, L.E.2    Cadenas, E.3    Poderoso, J.J.4
  • 41
    • 32644445476 scopus 로고    scopus 로고
    • Mitochondrial function and mitochondria-induced apoptosis in an overstimulated rat ovarian cycle
    • [41] Navarro, A., Torrejon, R., Bandez, M.J., Lopez-Cepero, J.M., Boveris, A., Mitochondrial function and mitochondria-induced apoptosis in an overstimulated rat ovarian cycle. Am. J. Physiol. Endocrinol. Metab. 289 (2005), E1101–E1109 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16014352.
    • (2005) Am. J. Physiol. Endocrinol. Metab. , vol.289 , pp. E1101-E1109
    • Navarro, A.1    Torrejon, R.2    Bandez, M.J.3    Lopez-Cepero, J.M.4    Boveris, A.5
  • 42
    • 6344289360 scopus 로고    scopus 로고
    • Rat brain and liver mitochondria develop oxidative stress and lose enzymatic activities on aging
    • [42] Navarro, A., Boveris, A., Rat brain and liver mitochondria develop oxidative stress and lose enzymatic activities on aging. Am. J. Physiol. Regul. Integr. Comp. Physiol. 287 (2004), R1244–R1249 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15271654.
    • (2004) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.287 , pp. R1244-R1249
    • Navarro, A.1    Boveris, A.2
  • 43
    • 33847059997 scopus 로고    scopus 로고
    • The mitochondrial energy transduction system and the aging process
    • [43] Navarro, A., Boveris, A., The mitochondrial energy transduction system and the aging process. Am. J. Physiol. Cell Physiol. 292 (2007), C670–C686 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=17020935.
    • (2007) Am. J. Physiol. Cell Physiol. , vol.292 , pp. C670-C686
    • Navarro, A.1    Boveris, A.2
  • 44
    • 0000517277 scopus 로고
    • Energy-linked reduction of NAD+ by succinate
    • [44] Ernster, L., Lee, C., Energy-linked reduction of NAD+ by succinate. Methods Enzym. X (1967), 729–738.
    • (1967) Methods Enzym. , vol.10 , pp. 729-738
    • Ernster, L.1    Lee, C.2
  • 45
    • 0023505509 scopus 로고
    • Endothelium-derived relaxing factor produced and released from artery and vein is nitric oxide
    • [45] Ignarro, L.J., Buga, G.M., Wood, K.S., Byrns, R.E., Chaudhuri, G., Endothelium-derived relaxing factor produced and released from artery and vein is nitric oxide. Proc. Natl. Acad. Sci. U. S. A. 84 (1987), 9265–9269 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=2827174.
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 9265-9269
    • Ignarro, L.J.1    Buga, G.M.2    Wood, K.S.3    Byrns, R.E.4    Chaudhuri, G.5
  • 46
    • 0028364425 scopus 로고
    • Nitric oxide assay using hemoglobin method
    • [46] Murphy, M.E., Noack, E., Nitric oxide assay using hemoglobin method. Methods Enzym 233 (1994), 240–250.
    • (1994) Methods Enzym , vol.233 , pp. 240-250
    • Murphy, M.E.1    Noack, E.2
  • 47
    • 0028245391 scopus 로고
    • Nitric-oxide synthase assays
    • [47] Hevel, J.M., Marletta, M.A., Nitric-oxide synthase assays. Methods Enzym 233 (1994), 250–258 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7516999.
    • (1994) Methods Enzym , vol.233 , pp. 250-258
    • Hevel, J.M.1    Marletta, M.A.2
  • 49
    • 0020484363 scopus 로고
    • Kinetics of ubiquinol-1-cytochrome c reductase in bovine heart mitochondria and submitochondrial particles
    • [49] Degli Espositi, M., Lenaz, G., Kinetics of ubiquinol-1-cytochrome c reductase in bovine heart mitochondria and submitochondrial particles. Biochim. Biophys. Acta 682 (1982), 189–200.
    • (1982) Biochim. Biophys. Acta , vol.682 , pp. 189-200
    • Degli Espositi, M.1    Lenaz, G.2
  • 50
    • 0036281179 scopus 로고    scopus 로고
    • Regulation of the rate of synthesis of nitric oxide by Mg(2+) and hypoxia. Studies in rat heart mitochondria
    • [50] Manzo-Avalos, S., Perez-Vazquez, V., Ramirez, J., Aguilera-Aguirre, L., Gonzalez-Hernandez, J.C., Clemente-Guerrero, M., et al. Regulation of the rate of synthesis of nitric oxide by Mg(2+) and hypoxia. Studies in rat heart mitochondria. Amino Acids 22 (2002), 381–389 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12107764.
    • (2002) Amino Acids , vol.22 , pp. 381-389
    • Manzo-Avalos, S.1    Perez-Vazquez, V.2    Ramirez, J.3    Aguilera-Aguirre, L.4    Gonzalez-Hernandez, J.C.5    Clemente-Guerrero, M.6
  • 51
    • 27744475763 scopus 로고    scopus 로고
    • Determination of mitochondrial nitric oxide synthase activity
    • [51] Ghafourifar, P., Asbury, M.L., Joshi, S.S., Kincaid, E.D., Determination of mitochondrial nitric oxide synthase activity. Methods Enzym 396 (2005), 424–444 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=16291251.
    • (2005) Methods Enzym , vol.396 , pp. 424-444
    • Ghafourifar, P.1    Asbury, M.L.2    Joshi, S.S.3    Kincaid, E.D.4
  • 52
    • 0035425503 scopus 로고    scopus 로고
    • Nitric oxide synthases: structure, function and inhibition
    • [52] Alderton, W.K., Cooper, C.E., Knowles, R.G., Nitric oxide synthases: structure, function and inhibition. Biochem. J. 357 (2001), 593–615 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=11463332.
    • (2001) Biochem. J. , vol.357 , pp. 593-615
    • Alderton, W.K.1    Cooper, C.E.2    Knowles, R.G.3
  • 53
    • 18844474423 scopus 로고    scopus 로고
    • Potentiometric analysis of the flavin cofactors of neuronal nitric oxide synthase
    • [53] Noble, M.A., Munro, A.W., Rivers, S.L., Robledo, L., Daff, S.N., Yellowlees, L.J., et al. Potentiometric analysis of the flavin cofactors of neuronal nitric oxide synthase. Biochemistry 38 (1999), 16413–16418 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10600101.
    • (1999) Biochemistry , vol.38 , pp. 16413-16418
    • Noble, M.A.1    Munro, A.W.2    Rivers, S.L.3    Robledo, L.4    Daff, S.N.5    Yellowlees, L.J.6
  • 54
    • 38649105151 scopus 로고    scopus 로고
    • Inactivation of mitochondrial respiratory chain complex I leads mitochondrial nitric oxide synthase to become pro-oxidative
    • [54] Parihar, M.S., Parihar, A., Villamena, F.A., Vaccaro, P.S., Ghafourifar, P., Inactivation of mitochondrial respiratory chain complex I leads mitochondrial nitric oxide synthase to become pro-oxidative. Biochem. Biophys. Res. Commun. 367 (2008), 761–767 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=18191636.
    • (2008) Biochem. Biophys. Res. Commun. , vol.367 , pp. 761-767
    • Parihar, M.S.1    Parihar, A.2    Villamena, F.A.3    Vaccaro, P.S.4    Ghafourifar, P.5
  • 55
    • 0037564168 scopus 로고    scopus 로고
    • Oxygen dependence of mitochondrial nitric oxide synthase activity
    • [55] Alvarez, S., Valdez, L.B., Zaobornyj, T., Boveris, A., Oxygen dependence of mitochondrial nitric oxide synthase activity. Biochem. Biophys. Res. Commun. 305 (2003), 771–775 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12763059.
    • (2003) Biochem. Biophys. Res. Commun. , vol.305 , pp. 771-775
    • Alvarez, S.1    Valdez, L.B.2    Zaobornyj, T.3    Boveris, A.4
  • 56
    • 78649982888 scopus 로고    scopus 로고
    • Effects of rotenone and pyridaben on complex I electron transfer and on mitochondrial nitric oxide synthase functional activity
    • [56] Navarro, A., Bandez, M.J., Gomez, C., Repetto, M.G., Boveris, A., Effects of rotenone and pyridaben on complex I electron transfer and on mitochondrial nitric oxide synthase functional activity. J. Bioenerg. Biomembr. 42 (2010), 405–412 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=20886364.
    • (2010) J. Bioenerg. Biomembr. , vol.42 , pp. 405-412
    • Navarro, A.1    Bandez, M.J.2    Gomez, C.3    Repetto, M.G.4    Boveris, A.5
  • 57
    • 76949089544 scopus 로고    scopus 로고
    • Brain mitochondrial dysfunction and oxidative damage in Parkinson's disease
    • [57] Navarro, A., Boveris, A., Brain mitochondrial dysfunction and oxidative damage in Parkinson's disease. J. Bioenerg. Biomembr. 41 (2009), 517–521 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=19915964.
    • (2009) J. Bioenerg. Biomembr. , vol.41 , pp. 517-521
    • Navarro, A.1    Boveris, A.2
  • 59
    • 84911466192 scopus 로고    scopus 로고
    • Ischaemic accumulation of succinate controls reperfusion injury through mitochondrial ROS
    • [59] Chouchani, E.T., Pell, V.R., Gaude, E., Aksentijević, D., Sundier, S.Y., Robb, E.L., et al. Ischaemic accumulation of succinate controls reperfusion injury through mitochondrial ROS. Nature 515 (2015), 431–435, 10.1038/nature13909.Ischaemic.
    • (2015) Nature , vol.515 , pp. 431-435
    • Chouchani, E.T.1    Pell, V.R.2    Gaude, E.3    Aksentijević, D.4    Sundier, S.Y.5    Robb, E.L.6
  • 60
    • 80051784790 scopus 로고    scopus 로고
    • The regulation of cell energetics and mitochondrial signaling by nitric oxide
    • second ed Elsevier Accademic Press London
    • [60] Boveris, A., Carreras, M.C., Poderoso, J.J., The regulation of cell energetics and mitochondrial signaling by nitric oxide. Nitric Oxide Biol. and Pathobiol, second ed, 2010, Elsevier Accademic Press, London, 441-482.
    • (2010) Nitric Oxide Biol. and Pathobiol , pp. 441-482
    • Boveris, A.1    Carreras, M.C.2    Poderoso, J.J.3
  • 61
    • 0035477926 scopus 로고    scopus 로고
    • Nitric oxide inhibits mitochondrial NADH:ubiquinone reductase activity through peroxynitrite formation
    • [61] Riobo, N.A., Clementi, E., Melani, M., Boveris, A., Cadenas, E., Moncada, S., et al. Nitric oxide inhibits mitochondrial NADH:ubiquinone reductase activity through peroxynitrite formation. Biochem. J. 359 (2001), 139–145 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=11563977.
    • (2001) Biochem. J. , vol.359 , pp. 139-145
    • Riobo, N.A.1    Clementi, E.2    Melani, M.3    Boveris, A.4    Cadenas, E.5    Moncada, S.6
  • 62
    • 3543008400 scopus 로고    scopus 로고
    • Inhibition of mitochondrial respiratory complex I by nitric oxide, peroxynitrite and S-nitrosothiols
    • [62] Brown, G.C., Borutaite, V., Inhibition of mitochondrial respiratory complex I by nitric oxide, peroxynitrite and S-nitrosothiols. Biochim. Biophys. Acta 1658 (2004), 44–49 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15282173.
    • (2004) Biochim. Biophys. Acta , vol.1658 , pp. 44-49
    • Brown, G.C.1    Borutaite, V.2
  • 63
    • 84902242573 scopus 로고    scopus 로고
    • Mitochondrial respiratory chain complexes as sources and targets of thiol-based redox-regulation
    • [63] Dröse, S., Brandt, U., Wittig, I., Mitochondrial respiratory chain complexes as sources and targets of thiol-based redox-regulation. Biochim. Biophys. Acta - Proteins Proteomics 1844 (2014), 1344–1354, 10.1016/j.bbapap.2014.02.006.
    • (2014) Biochim. Biophys. Acta - Proteins Proteomics , vol.1844 , pp. 1344-1354
    • Dröse, S.1    Brandt, U.2    Wittig, I.3
  • 64
    • 79961008706 scopus 로고    scopus 로고
    • Evidence for two sites of superoxide production by mitochondrial NADH-ubiquinone oxidoreductase (complex I)
    • [64] Treberg, J.R., Quinlan, C.L., Brand, M.D., Evidence for two sites of superoxide production by mitochondrial NADH-ubiquinone oxidoreductase (complex I). J. Biol. Chem. 286 (2011), 27103–27110, 10.1074/jbc.M111.252502.
    • (2011) J. Biol. Chem. , vol.286 , pp. 27103-27110
    • Treberg, J.R.1    Quinlan, C.L.2    Brand, M.D.3
  • 65
    • 84911476354 scopus 로고    scopus 로고
    • Generator-specific targets of mitochondrial reactive oxygen species
    • [65] Bleier, L., Wittig, I., Heide, H., Steger, M., Brandt, U., Dröse, S., Generator-specific targets of mitochondrial reactive oxygen species. Free Radic. Biol. Med. 78 (2015), 1–10, 10.1016/j.freeradbiomed.2014.10.511.
    • (2015) Free Radic. Biol. Med. , vol.78 , pp. 1-10
    • Bleier, L.1    Wittig, I.2    Heide, H.3    Steger, M.4    Brandt, U.5    Dröse, S.6
  • 66
    • 5344247921 scopus 로고    scopus 로고
    • Mitochondrial nitric oxide metabolism in rat muscle during endotoxemia
    • [66] Alvarez, S., Boveris, A., Mitochondrial nitric oxide metabolism in rat muscle during endotoxemia. Free Radic. Biol. Med. 37 (2004), 1472–1478 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15454287.
    • (2004) Free Radic. Biol. Med. , vol.37 , pp. 1472-1478
    • Alvarez, S.1    Boveris, A.2
  • 67
    • 84863866559 scopus 로고    scopus 로고
    • Endotoxemia impairs heart mitochondrial function by decreasing electron transfer, ATP synthesis and ATP content without affecting membrane potential
    • [67] Vanasco, V., Magnani, N.D., Cimolai, M.C., Valdez, L.B., Evelson, P., Boveris, A., et al. Endotoxemia impairs heart mitochondrial function by decreasing electron transfer, ATP synthesis and ATP content without affecting membrane potential. J. Bioenerg. Biomembr. 44 (2012), 243–252 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=22426814.
    • (2012) J. Bioenerg. Biomembr. , vol.44 , pp. 243-252
    • Vanasco, V.1    Magnani, N.D.2    Cimolai, M.C.3    Valdez, L.B.4    Evelson, P.5    Boveris, A.6
  • 69
    • 60549083568 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in neurodegenerative diseases
    • [69] Schapira, A.H.V., Mitochondrial dysfunction in neurodegenerative diseases. Neurochem. Res. 33 (2008), 2502–2509, 10.1007/s11064-008-9855-x.
    • (2008) Neurochem. Res. , vol.33 , pp. 2502-2509
    • Schapira, A.H.V.1


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