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Volumn 1777, Issue 5, 2008, Pages 470-476

Nitric oxide degradation by potato tuber mitochondria: Evidence for the involvement of external NAD(P)H dehydrogenases

Author keywords

Electron leakage; External NAD(P)H dehydrogenases; Nitric oxide degradation; Plant mitochondria; Potato tuber; Superoxide anion

Indexed keywords

ANTIMYCIN A1; CALCIUM ION; MALIC ACID; MYXOTHIAZOL; NITRIC OXIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE DEHYDROGENASE; SUCCINIC ACID; SUPEROXIDE DISMUTASE;

EID: 43049095110     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2008.02.006     Document Type: Article
Times cited : (39)

References (46)
  • 1
    • 1842716716 scopus 로고    scopus 로고
    • Nitric oxide and nitric oxide synthase activity in plants
    • del Rio L.A., Corpas F.J., and Barroso J.B. Nitric oxide and nitric oxide synthase activity in plants. Phytochemistry 65 (2004) 783-792
    • (2004) Phytochemistry , vol.65 , pp. 783-792
    • del Rio, L.A.1    Corpas, F.J.2    Barroso, J.B.3
  • 3
    • 0032490943 scopus 로고    scopus 로고
    • Nitric oxide functions as a signal in plant disease resistance
    • Delledonne M., Xia Y., Dixon R.A., and Lamb C. Nitric oxide functions as a signal in plant disease resistance. Nature 394 (1998) 585-588
    • (1998) Nature , vol.394 , pp. 585-588
    • Delledonne, M.1    Xia, Y.2    Dixon, R.A.3    Lamb, C.4
  • 4
    • 0036851190 scopus 로고    scopus 로고
    • Nitric oxide synthase-mediated phytoalexin accumulation in soybean cotyledons in response to the Diaporthe phaseolorum f. sp. meridionalis elicitor
    • Modolo L.V., Cunha F.Q., Braga M.R., and Salgado I. Nitric oxide synthase-mediated phytoalexin accumulation in soybean cotyledons in response to the Diaporthe phaseolorum f. sp. meridionalis elicitor. Plant Physiol. 130 (2002) 1288-1297
    • (2002) Plant Physiol. , vol.130 , pp. 1288-1297
    • Modolo, L.V.1    Cunha, F.Q.2    Braga, M.R.3    Salgado, I.4
  • 5
    • 33747429121 scopus 로고    scopus 로고
    • Decreased arginine and nitrite levels in nitrate reductase-deficient Arabidopsis thaliana plants impair nitric oxide synthesis and the hypersensitive response to Pseudomonas syringae
    • Modolo L.V., Augusto O., Almeida I.M.G., Pinto-Maglio C.A.F., Oliveira H.C., Seligman K., and Salgado I. Decreased arginine and nitrite levels in nitrate reductase-deficient Arabidopsis thaliana plants impair nitric oxide synthesis and the hypersensitive response to Pseudomonas syringae. Plant Sci. 171 (2006) 34-40
    • (2006) Plant Sci. , vol.171 , pp. 34-40
    • Modolo, L.V.1    Augusto, O.2    Almeida, I.M.G.3    Pinto-Maglio, C.A.F.4    Oliveira, H.C.5    Seligman, K.6    Salgado, I.7
  • 7
    • 0028100682 scopus 로고
    • Kinetics of nitric oxide autoxidation in aqueous solutions
    • Kharitonov V.G., Sundquist A.R., and Sharma V.S. Kinetics of nitric oxide autoxidation in aqueous solutions. J. Biol. Chem. 269 (1994) 5881-5883
    • (1994) J. Biol. Chem. , vol.269 , pp. 5881-5883
    • Kharitonov, V.G.1    Sundquist, A.R.2    Sharma, V.S.3
  • 9
    • 10644291828 scopus 로고    scopus 로고
    • Nitric oxide dioxygenase function and mechanism of flavohemoglobin, hemoglobin, myoglobin and their associated reductases
    • Gardner P.R. Nitric oxide dioxygenase function and mechanism of flavohemoglobin, hemoglobin, myoglobin and their associated reductases. J. Inorg. Biochem. 99 (2005) 247-266
    • (2005) J. Inorg. Biochem. , vol.99 , pp. 247-266
    • Gardner, P.R.1
  • 10
    • 0029963244 scopus 로고    scopus 로고
    • Rapid reduction of nitric oxide by mitochondria, and reversibly inhibition of mitochondrial respiration by nitric oxide
    • Borutaite V., and Brown G.C. Rapid reduction of nitric oxide by mitochondria, and reversibly inhibition of mitochondrial respiration by nitric oxide. Biochem. J. 315 (1996) 295-299
    • (1996) Biochem. J. , vol.315 , pp. 295-299
    • Borutaite, V.1    Brown, G.C.2
  • 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
    • Cleeter M.W., Cooper J.M., Darley-Usmar V.M., Moncada S., and 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
    • (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
    • 0036889794 scopus 로고    scopus 로고
    • Nitric oxide inhibition of mitochondrial respiration and its role in cell death
    • Brown G.C., and Borutaite V. Nitric oxide inhibition of mitochondrial respiration and its role in cell death. Free Radic. Biol. Med. 33 (2002) 1440-1450
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 1440-1450
    • Brown, G.C.1    Borutaite, V.2
  • 13
    • 0030566801 scopus 로고    scopus 로고
    • Nitric oxide inhibits the cytochrome oxidase but not the alternative oxidase of plant mitochondria
    • Millar A.H., and Day D.A. Nitric oxide inhibits the cytochrome oxidase but not the alternative oxidase of plant mitochondria. FEBS Lett. 398 (1996) 155-158
    • (1996) FEBS Lett. , vol.398 , pp. 155-158
    • Millar, A.H.1    Day, D.A.2
  • 14
    • 0034968202 scopus 로고    scopus 로고
    • Inhibitory effects of nitric oxide on oxidative phosphorylation in plant mitochondria
    • Yamasaki H., Shimoji H., Ohshiro Y., and Sakihama Y. Inhibitory effects of nitric oxide on oxidative phosphorylation in plant mitochondria. Nitric Oxide Biol. Chem. 5 (2001) 261-270
    • (2001) Nitric Oxide Biol. Chem. , vol.5 , pp. 261-270
    • Yamasaki, H.1    Shimoji, H.2    Ohshiro, Y.3    Sakihama, Y.4
  • 15
    • 0037116605 scopus 로고    scopus 로고
    • Participation of the mitochondrial permeability transition pore in nitric oxide-induced plant cell death
    • Saviani E.E., Orsi C.H., Oliveira J.F.P., Pinto-Maglio C.A.F., and Salgado I. Participation of the mitochondrial permeability transition pore in nitric oxide-induced plant cell death. FEBS Lett. 510 (2002) 136-140
    • (2002) FEBS Lett. , vol.510 , pp. 136-140
    • Saviani, E.E.1    Orsi, C.H.2    Oliveira, J.F.P.3    Pinto-Maglio, C.A.F.4    Salgado, I.5
  • 17
    • 0029986691 scopus 로고    scopus 로고
    • Nitric oxide inhibits electron transfer and increases superoxide radical production in rat heart mitochondria and submitochondrial particles
    • Poderoso J.J., Carreras M.C., Lisdero C., Riobó N., Schöpfer F., and 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
    • (1996) Arch. Biochem. Biophys. , vol.328 , pp. 85-92
    • Poderoso, J.J.1    Carreras, M.C.2    Lisdero, C.3    Riobó, N.4    Schöpfer, F.5    Boveris, A.6
  • 19
  • 20
    • 33744963444 scopus 로고    scopus 로고
    • Direct and indirect roles of cytochrome b in the mediation of superoxide generation and NO catabolism by mitochondrial succinate-cytochrome c reductase
    • Chen Y.R., Chen C.L., Yeh A., Liu X., and Zweier J.L. Direct and indirect roles of cytochrome b in the mediation of superoxide generation and NO catabolism by mitochondrial succinate-cytochrome c reductase. J. Biol. Chem. 291 (2006) 13159-13168
    • (2006) J. Biol. Chem. , vol.291 , pp. 13159-13168
    • Chen, Y.R.1    Chen, C.L.2    Yeh, A.3    Liu, X.4    Zweier, J.L.5
  • 21
    • 0035781005 scopus 로고    scopus 로고
    • Plant mitochondria and oxidative stress: electron transport, NADPH turnover, and metabolism of reactive oxygen species
    • Moller I.M. Plant mitochondria and oxidative stress: electron transport, NADPH turnover, and metabolism of reactive oxygen species. Annu. Rev. Plant Physiol. Plant Mol. Biol. 52 (2001) 561-591
    • (2001) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.52 , pp. 561-591
    • Moller, I.M.1
  • 22
    • 0037265815 scopus 로고    scopus 로고
    • The alternative oxidase: in vivo regulation and function
    • Millenaar F.F., and Lambers H. The alternative oxidase: in vivo regulation and function. Plant Biol. 5 (2003) 2-15
    • (2003) Plant Biol. , vol.5 , pp. 2-15
    • Millenaar, F.F.1    Lambers, H.2
  • 24
    • 0027762128 scopus 로고
    • Biological activity of S-nitrosothiols: the role of nitric oxide
    • Mathews W.R., and Kerr S.W. Biological activity of S-nitrosothiols: the role of nitric oxide. J. Pharmacol. Exp. Ther. 267 (1993) 1529-1537
    • (1993) J. Pharmacol. Exp. Ther. , vol.267 , pp. 1529-1537
    • Mathews, W.R.1    Kerr, S.W.2
  • 25
    • 0000087998 scopus 로고
    • Purification, characterization and storage of mitochondria from Jerusalem artichoke tubers
    • Lindén A.C., and Moller I.M. Purification, characterization and storage of mitochondria from Jerusalem artichoke tubers. Physiol. Plant. 72 (1988) 265-270
    • (1988) Physiol. Plant. , vol.72 , pp. 265-270
    • Lindén, A.C.1    Moller, I.M.2
  • 26
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 27
    • 21644442197 scopus 로고    scopus 로고
    • Real time and in vivo monitoring of nitric oxide by electrochemical sensors-from dream to reality
    • Zhang X. Real time and in vivo monitoring of nitric oxide by electrochemical sensors-from dream to reality. Front. Biosci. 9 (2004) 3434-3446
    • (2004) Front. Biosci. , vol.9 , pp. 3434-3446
    • Zhang, X.1
  • 28
    • 0017201717 scopus 로고
    • Safranine as a probe of the mitochondrial membrane potential
    • Akerman K.E.O., and Wikström M.K.F. Safranine as a probe of the mitochondrial membrane potential. FEBS Lett. 68 (1976) 191-197
    • (1976) FEBS Lett. , vol.68 , pp. 191-197
    • Akerman, K.E.O.1    Wikström, M.K.F.2
  • 29
    • 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
    • Zhou M., Diwu Z., Panchuk-Voloshina N., and Haugland R.P. 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
    • (1997) Anal. Biochem. , vol.253 , pp. 162-168
    • Zhou, M.1    Diwu, Z.2    Panchuk-Voloshina, N.3    Haugland, R.P.4
  • 30
    • 33744527052 scopus 로고    scopus 로고
    • Persistent S-nitrosation of complex I and other mitochondrial membrane proteins by S-nitrosothiols but not nitric oxide or peroxynitrite
    • Dahm C.C., Moore K., and Murphy M.P. Persistent S-nitrosation of complex I and other mitochondrial membrane proteins by S-nitrosothiols but not nitric oxide or peroxynitrite. J. Biol. Chem. 281 (2006) 10056-10065
    • (2006) J. Biol. Chem. , vol.281 , pp. 10056-10065
    • Dahm, C.C.1    Moore, K.2    Murphy, M.P.3
  • 31
    • 0037441390 scopus 로고    scopus 로고
    • External alternative NADH dehydrogenase of Saccharomyces cerevisiae: a potential source of superoxide
    • Fang J., and Beattie D.S. External alternative NADH dehydrogenase of Saccharomyces cerevisiae: a potential source of superoxide. Free Radic. Biol. Med. 34 (2003) 478-488
    • (2003) Free Radic. Biol. Med. , vol.34 , pp. 478-488
    • Fang, J.1    Beattie, D.S.2
  • 32
    • 10344221083 scopus 로고    scopus 로고
    • Complex III releases superoxide to both sides of the inner mitochondrial membrane
    • Muller F.L., Liu Y., and Remmen H.V. Complex III releases superoxide to both sides of the inner mitochondrial membrane. J. Biol. Chem. 27 (2004) 49064-49073
    • (2004) J. Biol. Chem. , vol.27 , pp. 49064-49073
    • Muller, F.L.1    Liu, Y.2    Remmen, H.V.3
  • 33
    • 33745628757 scopus 로고    scopus 로고
    • Generation of superoxide by the mitochondrial complex I
    • Grivennikova V.G., and Vinogradov A.D. Generation of superoxide by the mitochondrial complex I. Biochim. Biophys. Acta 1747 (2006) 553-561
    • (2006) Biochim. Biophys. Acta , vol.1747 , pp. 553-561
    • Grivennikova, V.G.1    Vinogradov, A.D.2
  • 34
    • 0141815741 scopus 로고    scopus 로고
    • Production of reactive oxygen species by mitochondria: central role of complex III
    • Chen Q., Vazquez E.J., Moghaddas S., Hoppel C.L., and Lesnefsky E.J. Production of reactive oxygen species by mitochondria: central role of complex III. J. Biol. Chem. 278 (2003) 36027-36031
    • (2003) J. Biol. Chem. , vol.278 , pp. 36027-36031
    • Chen, Q.1    Vazquez, E.J.2    Moghaddas, S.3    Hoppel, C.L.4    Lesnefsky, E.J.5
  • 37
    • 0017818494 scopus 로고
    • The sites of superoxide anion generation in higher plant mitochondria
    • Rich P.R., and Bonner W.D. The sites of superoxide anion generation in higher plant mitochondria. Arch. Biochem. Biophys. 188 (1978) 206-213
    • (1978) Arch. Biochem. Biophys. , vol.188 , pp. 206-213
    • Rich, P.R.1    Bonner, W.D.2
  • 38
    • 0028851042 scopus 로고
    • Superoxide production by mitochondria isolated from green bell pepper fruit
    • Purvis A.C., Shewfelt R.L., and Gegogeine J.W. Superoxide production by mitochondria isolated from green bell pepper fruit. Physiol. Plant. 94 (1995) 743-749
    • (1995) Physiol. Plant. , vol.94 , pp. 743-749
    • Purvis, A.C.1    Shewfelt, R.L.2    Gegogeine, J.W.3
  • 39
    • 0028177211 scopus 로고
    • 2{radical dot}- in the production of HO{radical dot}: in vitro and in vivo
    • 2{radical dot}- in the production of HO{radical dot}: in vitro and in vivo. Free Radic. Biol. Med. 16 (1994) 29-33
    • (1994) Free Radic. Biol. Med. , vol.16 , pp. 29-33
    • Liochev, S.I.1    Fridovich, I.2
  • 41
    • 21244453184 scopus 로고    scopus 로고
    • Nitrite as the major source of nitric oxide production by Arabidopsis thaliana in response to Pseudomonas syringae
    • Modolo L.V., Augusto O., Almeida I.M., Magalhaes J.R., and Salgado I. Nitrite as the major source of nitric oxide production by Arabidopsis thaliana in response to Pseudomonas syringae. FEBS Lett. 579 (2005) 3814-3820
    • (2005) FEBS Lett. , vol.579 , pp. 3814-3820
    • Modolo, L.V.1    Augusto, O.2    Almeida, I.M.3    Magalhaes, J.R.4    Salgado, I.5
  • 42
    • 14844289535 scopus 로고    scopus 로고
    • Nitric oxide emission from tobacco leaves and cell suspensions: rate limiting factors and evidence for the involvement of mitochondrial electron transport
    • Planchet E., Gupta K.J., Sonoda M., and Kaiser W.M. Nitric oxide emission from tobacco leaves and cell suspensions: rate limiting factors and evidence for the involvement of mitochondrial electron transport. Plant J. 41 (2005) 732-743
    • (2005) Plant J. , vol.41 , pp. 732-743
    • Planchet, E.1    Gupta, K.J.2    Sonoda, M.3    Kaiser, W.M.4
  • 44
    • 33751110470 scopus 로고    scopus 로고
    • Chloroplasts as a nitric oxide cellular source. Effect of reactive nitrogen species and chloroplastic lipids and proteins
    • Jasid S., Simontacchi M., Bartoli C.G., and Puntarulo S. Chloroplasts as a nitric oxide cellular source. Effect of reactive nitrogen species and chloroplastic lipids and proteins. Plant Physiol. 142 (2006) 1246-1255
    • (2006) Plant Physiol. , vol.142 , pp. 1246-1255
    • Jasid, S.1    Simontacchi, M.2    Bartoli, C.G.3    Puntarulo, S.4
  • 45
    • 0033952545 scopus 로고    scopus 로고
    • Simultaneous production of nitric oxide and peroxynitrite by plant nitrate reductase: in vitro evidence for the NR-dependent formation of active nitrogen species
    • Yamasaki H., and Sakihama Y. Simultaneous production of nitric oxide and peroxynitrite by plant nitrate reductase: in vitro evidence for the NR-dependent formation of active nitrogen species. FEBS Lett. 468 (2000) 89-92
    • (2000) FEBS Lett. , vol.468 , pp. 89-92
    • Yamasaki, H.1    Sakihama, Y.2
  • 46
    • 0035037361 scopus 로고    scopus 로고
    • A plasma membrane-bound enzyme of tobacco roots catalyses the formation of nitric oxide from nitrite
    • Stöhr C., Strube F., Marx G., Ullrich W.R., and Rockel P. A plasma membrane-bound enzyme of tobacco roots catalyses the formation of nitric oxide from nitrite. Planta 212 (2001) 835-841
    • (2001) Planta , vol.212 , pp. 835-841
    • Stöhr, C.1    Strube, F.2    Marx, G.3    Ullrich, W.R.4    Rockel, P.5


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