메뉴 건너뛰기




Volumn 380, Issue 1, 2004, Pages 193-202

Oxidation and reduction of pyridine nucleotides in alamethicin- permeabilized plant mitochondria

Author keywords

Alamethicin; Complex I; Electron transport chain; NADH dehydrogenase; Permeabilization; Plant mitochondria

Indexed keywords

ELECTRON TRANSPORT PROPERTIES; METABOLITES; OXIDATION; PLANTS (BOTANY); REDUCTION; SUBSTRATES;

EID: 2642545691     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20031969     Document Type: Article
Times cited : (32)

References (42)
  • 1
    • 0002967443 scopus 로고    scopus 로고
    • Metabolite exchange between the mitochondrion and the cytosol
    • Dennis, D. T., Turpin, D. H., Lefebvre, D. D. and Layzell, D. B., eds., Addison Wesley Longman Ltd, London
    • Douce, R., Aubert, S. and Neuburger, M. (1997) Metabolite exchange between the mitochondrion and the cytosol. In Plant Metabolism (Dennis, D. T., Turpin, D. H., Lefebvre, D. D. and Layzell, D. B., eds.), pp. 234-251, Addison Wesley Longman Ltd, London
    • (1997) Plant Metabolism , pp. 234-251
    • Douce, R.1    Aubert, S.2    Neuburger, M.3
  • 2
    • 0028226051 scopus 로고
    • Alamethicin: A peptide model for voltage gating and protein-membrane interactions
    • Cafiso, D. S. (1994) Alamethicin: a peptide model for voltage gating and protein-membrane interactions. Annu. Rev. Biophys. Biomol. Struct. 23, 141-165
    • (1994) Annu. Rev. Biophys. Biomol. Struct. , vol.23 , pp. 141-165
    • Cafiso, D.S.1
  • 3
    • 0035498468 scopus 로고    scopus 로고
    • Voltage-dependent pore formation and antimicrobial activity by alamethicin and analogues
    • Duclohier, H. and Wróblewski, H. (2001) Voltage-dependent pore formation and antimicrobial activity by alamethicin and analogues. J. Membr. Biol. 184, 1-12
    • (2001) J. Membr. Biol. , vol.184 , pp. 1-12
    • Duclohier, H.1    Wróblewski, H.2
  • 5
    • 0035937792 scopus 로고    scopus 로고
    • Catalytic activity of NADH-ubiquinone oxidoreductase (complex I) in intact mitochondria - Evidence for the slow active/inactive transition
    • Grivennikova, V. G., Kapustin, A. N. and Vinogradov, A. D. (2001) Catalytic activity of NADH-ubiquinone oxidoreductase (complex I) in intact mitochondria - evidence for the slow active/inactive transition. J. Biol. Chem. 276, 9038-9044
    • (2001) J. Biol. Chem. , vol.276 , pp. 9038-9044
    • Grivennikova, V.G.1    Kapustin, A.N.2    Vinogradov, A.D.3
  • 6
    • 0037328645 scopus 로고    scopus 로고
    • In situ assay of the intramitochondrial enzymes: Use of alamethicin for permeabilization of mitochondria
    • Gostimskaya, I. S., Grivennikova, V. G., Zharova, T. V., Bakeeva, L. E. and Vinogradov, A. D. (2003) In situ assay of the intramitochondrial enzymes: use of alamethicin for permeabilization of mitochondria. Anal. Biochem. 313, 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
  • 7
    • 0036788293 scopus 로고    scopus 로고
    • Dysfunction of mitochondria in human skeletal muscle in type 2 diabetes
    • Kelley, D. E., He, J., Menshikova, E. V. and Ritov, V. B. (2002) Dysfunction of mitochondria in human skeletal muscle in type 2 diabetes. Diabetes 51, 2944-2950
    • (2002) Diabetes , vol.51 , pp. 2944-2950
    • Kelley, D.E.1    He, J.2    Menshikova, E.V.3    Ritov, V.B.4
  • 8
    • 0032490088 scopus 로고    scopus 로고
    • Physiological, biochemical and molecular aspects of mitochondrial complex I in plants
    • Rasmusson, A. G., Heiser, V., Zabaleta, E., Brennicke, A. and Grohmann, L. (1998) Physiological, biochemical and molecular aspects of mitochondrial complex I in plants. Biochim. Biophys. Acta 1364, 101-111
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 101-111
    • Rasmusson, A.G.1    Heiser, V.2    Zabaleta, E.3    Brennicke, A.4    Grohmann, L.5
  • 9
    • 0035781005 scopus 로고    scopus 로고
    • Plant mitochondria and oxidative stress: Electron transport, NADPH turnover, and metabolism of reactive oxygen species
    • Møller, I. M. (2001) Plant mitochondria and oxidative stress: electron transport, NADPH turnover, and metabolism of reactive oxygen species. Annu. Rev. Plant Physiol. Plant Mol. Biol. 52, 561-591
    • (2001) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.52 , pp. 561-591
    • Møller, I.M.1
  • 10
    • 84986974453 scopus 로고
    • Direct evidence for the presence of a rotenone-resistant NADH dehydrogenase on the inner surface of the inner membrane of plant mitochondria
    • Møller, I. M. and Palmer, J. M. (1982) Direct evidence for the presence of a rotenone-resistant NADH dehydrogenase on the inner surface of the inner membrane of plant mitochondria. Physiol. Plant. 54, 267-274
    • (1982) Physiol. Plant. , vol.54 , pp. 267-274
    • Møller, I.M.1    Palmer, J.M.2
  • 11
    • 84989674612 scopus 로고
    • NAD(P)H dehydrogenases on the inner surface of the inner mitochondrial membrane studied using inside-out submitochondrial particles
    • Rasmusson, A. G. and Møller, I. M. (1991) NAD(P)H dehydrogenases on the inner surface of the inner mitochondrial membrane studied using inside-out submitochondrial particles. Physiol. Plant. 83, 357-365
    • (1991) Physiol. Plant. , vol.83 , pp. 357-365
    • Rasmusson, A.G.1    Møller, I.M.2
  • 12
    • 0025932019 scopus 로고
    • Effect of calcium ions and inhibitors on internal NAD(P)H dehydrogenases in plant mitochondria
    • Rasmusson, A. G. and Møller, I. M. (1991) Effect of calcium ions and inhibitors on internal NAD(P)H dehydrogenases in plant mitochondria. Eur. J. Biochem. 202, 617-623
    • (1991) Eur. J. Biochem. , vol.202 , pp. 617-623
    • Rasmusson, A.G.1    Møller, I.M.2
  • 13
    • 0030581482 scopus 로고    scopus 로고
    • Evidence for the presence of two rotenone-insensitive NAD(P)H dehydrogenases on the inner surface of the inner membrane of potato tuber mitochondria
    • Melo, A. M. P., Roberts, T. H. and Møller, I. M. (1996) Evidence for the presence of two rotenone-insensitive NAD(P)H dehydrogenases on the inner surface of the inner membrane of potato tuber mitochondria. Biochim. Biophys. Acta 1276, 133-139
    • (1996) Biochim. Biophys. Acta , vol.1276 , pp. 133-139
    • Melo, A.M.P.1    Roberts, T.H.2    Møller, I.M.3
  • 14
    • 1042290216 scopus 로고    scopus 로고
    • Identification of a mitochondrial external NADPH dehydrogenase by overexpression in transgenic Nicotiana sylvestris
    • Michalecka, A. M., Agius, S. C., Møller, I. M. and Rasmusson, A. G. (2004) Identification of a mitochondrial external NADPH dehydrogenase by overexpression in transgenic Nicotiana sylvestris. Plant J. 37, 415-425
    • (2004) Plant J. , vol.37 , pp. 415-425
    • Michalecka, A.M.1    Agius, S.C.2    Møller, I.M.3    Rasmusson, A.G.4
  • 15
    • 0028862799 scopus 로고
    • Direct evidence for the presence of 2 external NAD(P)H dehydrogenases coupled to the electron transport chain in plant mitochondria
    • Roberts, T. H., Fredlund, K. M. and Møller, I. M. (1995) Direct evidence for the presence of 2 external NAD(P)H dehydrogenases coupled to the electron transport chain in plant mitochondria. FEBS Lett. 373, 307-309
    • (1995) FEBS Lett. , vol.373 , pp. 307-309
    • Roberts, T.H.1    Fredlund, K.M.2    Møller, I.M.3
  • 16
    • 84989741846 scopus 로고
    • The presence of a short redox chain in the membrane of intact potato tuber peroxisomes and the association of malate dehydrogenase with the peroxisomal membrane
    • Struglics, A., Fredlund, K. M., Rasmusson, A. G. and Møller, I. M. (1993) The presence of a short redox chain in the membrane of intact potato tuber peroxisomes and the association of malate dehydrogenase with the peroxisomal membrane. Physiol. Plant. 88, 19-28
    • (1993) Physiol. Plant. , vol.88 , pp. 19-28
    • Struglics, A.1    Fredlund, K.M.2    Rasmusson, A.G.3    Møller, I.M.4
  • 17
    • 0000636038 scopus 로고
    • Biochemical characterization of chlorophyll-free mitochondria from pea leaves
    • Day, D. A., Neuburger, M. and Douce, R. (1985) Biochemical characterization of chlorophyll-free mitochondria from pea leaves. Aust. J. Plant Physiol. 12, 219-228
    • (1985) Aust. J. Plant Physiol. , vol.12 , pp. 219-228
    • Day, D.A.1    Neuburger, M.2    Douce, R.3
  • 18
    • 0000032686 scopus 로고
    • Properties of substantially chlorophyll free pea leaf mitochondria prepared by sucrose density gradient separation
    • Nash, D. and Wiskich, J. T. (1983) Properties of substantially chlorophyll free pea leaf mitochondria prepared by sucrose density gradient separation. Plant Physiol. 71, 627-634
    • (1983) Plant Physiol. , vol.71 , pp. 627-634
    • Nash, D.1    Wiskich, J.T.2
  • 19
    • 0001844190 scopus 로고
    • Copper enzymes in isolated chloroplasts: Polyphenol oxidase in Beta vulgaris
    • Arnon, D. I. (1949) Copper enzymes in isolated chloroplasts: polyphenol oxidase in Beta vulgaris. Plant Physiol. 24, 1-15
    • (1949) Plant Physiol. , vol.24 , pp. 1-15
    • Arnon, D.I.1
  • 20
    • 0034782250 scopus 로고    scopus 로고
    • Light-dependent gene expression for proteins in the respiratory chain of potato leaves
    • Svensson, Å. S. and Rasmusson, A. G. (2001) Light-dependent gene expression for proteins in the respiratory chain of potato leaves. Plant J. 28, 73-82
    • (2001) Plant J. , vol.28 , pp. 73-82
    • Svensson, Å.S.1    Rasmusson, A.G.2
  • 21
    • 0000171468 scopus 로고
    • NADP-utilizing enzymes in the matrix of plant mitochondria
    • Rasmusson, A. G. and Møller, I. M. (1990) NADP-utilizing enzymes in the matrix of plant mitochondria. Plant Physiol. 94, 1012-1018
    • (1990) Plant Physiol. , vol.94 , pp. 1012-1018
    • Rasmusson, A.G.1    Møller, I.M.2
  • 22
    • 77957091719 scopus 로고
    • Isolation of submitochondrial particles with different polarities
    • Møller, I. M., Lidén, A. C., Ericson, I. and Gardeström, P. (1987) Isolation of submitochondrial particles with different polarities. Methods Enzymol. 148, 442-453
    • (1987) Methods Enzymol. , vol.148 , pp. 442-453
    • Møller, I.M.1    Lidén, A.C.2    Ericson, I.3    Gardeström, P.4
  • 23
    • 0001405510 scopus 로고
    • The regulation of malate oxidation in plant-mitochondria by the redox state of endogenous pyridine nucleotides
    • Neuburger, M., Day, D. A. and Douce, R. (1984) The regulation of malate oxidation in plant-mitochondria by the redox state of endogenous pyridine nucleotides. Physiol. Veg. 22, 571-580
    • (1984) Physiol. Veg. , vol.22 , pp. 571-580
    • Neuburger, M.1    Day, D.A.2    Douce, R.3
  • 25
    • 0029911102 scopus 로고    scopus 로고
    • Ubiquinone-1 induces external deamino-NADH oxidation in potato tuber mitochondria
    • Møller, I. M., Roberts, T. H. and Rasmusson, A. G. (1996) Ubiquinone-1 induces external deamino-NADH oxidation in potato tuber mitochondria. Plant Physiol. 112, 75-78
    • (1996) Plant Physiol. , vol.112 , pp. 75-78
    • Møller, I.M.1    Roberts, T.H.2    Rasmusson, A.G.3
  • 26
    • 0035680135 scopus 로고    scopus 로고
    • Rotenone-insensitive NAD(P)H dehydrogenases in plants: Immunodetection and distribution of native proteins in mitochondria
    • Rasmusson, A. G. and Agius, S. C. (2001) Rotenone-insensitive NAD(P)H dehydrogenases in plants: immunodetection and distribution of native proteins in mitochondria. Plant Physiol. Biochem. 39, 1057-1066
    • (2001) Plant Physiol. Biochem. , vol.39 , pp. 1057-1066
    • Rasmusson, A.G.1    Agius, S.C.2
  • 28
    • 0032812743 scopus 로고    scopus 로고
    • A single external enzyme confers alternative NADH: Ubiquinone oxidoreductase activity in Yarrowia lipolytica
    • Kerscher, S. J., Okun, J. G. and Brandt, U. (1999) A single external enzyme confers alternative NADH: ubiquinone oxidoreductase activity in Yarrowia lipolytica. J. Cell Sci. 112, 2347-2354
    • (1999) J. Cell Sci. , vol.112 , pp. 2347-2354
    • Kerscher, S.J.1    Okun, J.G.2    Brandt, U.3
  • 29
    • 0027978980 scopus 로고
    • Antibacterial peptides and mitochondrial presequences affect mitochondrial coupling, respiration and protein import
    • Hugosson, M., Andreu, D., Boman, H. G. and Glaser, E. (1994) Antibacterial peptides and mitochondrial presequences affect mitochondrial coupling, respiration and protein import. Eur. J. Biochem. 223, 1027-1033
    • (1994) Eur. J. Biochem. , vol.223 , pp. 1027-1033
    • Hugosson, M.1    Andreu, D.2    Boman, H.G.3    Glaser, E.4
  • 30
    • 0001075709 scopus 로고
    • Evidence for metabolic domains within the matrix compartment of pea leaf mitochondria - Implications for photorespiratory metabolism
    • Wiskich, J. T., Bryce, J. H., Day, D. A. and Dry, I. B. (1990) Evidence for metabolic domains within the matrix compartment of pea leaf mitochondria - implications for photorespiratory metabolism. Plant Physiol. 93, 611-616
    • (1990) Plant Physiol. , vol.93 , pp. 611-616
    • Wiskich, J.T.1    Bryce, J.H.2    Day, D.A.3    Dry, I.B.4
  • 31
    • 0033569439 scopus 로고    scopus 로고
    • Plant mitochondrial 2-oxoglutarate dehydrogenase complex: Purification and characterization in potato
    • Millar, A. H., Hill, S. A. and Leaver, C. J. (1999) Plant mitochondrial 2-oxoglutarate dehydrogenase complex: purification and characterization in potato. Biochem. J. 343, 327-334
    • (1999) Biochem. J. , vol.343 , pp. 327-334
    • Millar, A.H.1    Hill, S.A.2    Leaver, C.J.3
  • 32
    • 0027653748 scopus 로고
    • 17th Fritz Lipmann lecture. Wanderings (wonderings) in metabolism
    • Srere, P. A. (1993) 17th Fritz Lipmann lecture. Wanderings (wonderings) in metabolism. Biol. Chem. Hoppe Seyler 374, 833-842
    • (1993) Biol. Chem. Hoppe Seyler , vol.374 , pp. 833-842
    • Srere, P.A.1
  • 33
    • 0015928859 scopus 로고
    • External NADH dehydrogenases of intact plant mitochondria
    • Douce, R., Mannella, C. A. and Bonner, W. D. (1973) External NADH dehydrogenases of intact plant mitochondria. Biochim. Biophys. Acta 292, 105-116
    • (1973) Biochim. Biophys. Acta , vol.292 , pp. 105-116
    • Douce, R.1    Mannella, C.A.2    Bonner, W.D.3
  • 34
    • 0030469323 scopus 로고    scopus 로고
    • Identification and characterization of an inducible NAD(P)H dehydrogenase from red beetroot mitochondria
    • Menz, R. I. and Day, D. A. (1996) Identification and characterization of an inducible NAD(P)H dehydrogenase from red beetroot mitochondria. Plant Physiol. 112, 607-613
    • (1996) Plant Physiol. , vol.112 , pp. 607-613
    • Menz, R.I.1    Day, D.A.2
  • 35
    • 0029169788 scopus 로고
    • Purification, characterization, and submitochondrial localization of a 58-kilodalton NAD(P)H dehydrogenase
    • Luethy, M. H., Thelen, J. J., Knudten, A. F. and Elthon, T. E. (1995) Purification, characterization, and submitochondrial localization of a 58-kilodalton NAD(P)H dehydrogenase. Plant Physiol. 107, 443-450
    • (1995) Plant Physiol. , vol.107 , pp. 443-450
    • Luethy, M.H.1    Thelen, J.J.2    Knudten, A.F.3    Elthon, T.E.4
  • 36
    • 0033213361 scopus 로고    scopus 로고
    • Homologues of yeast and bacterial rotenone-insensitive NADH dehydrogenases in higher eukaryotes: Two enzymes are present in potato mitochondria
    • Rasmusson, A. G., Svensson, A. S., Knoop, V., Grohmann, L. and Brennicke, A. (1999) Homologues of yeast and bacterial rotenone-insensitive NADH dehydrogenases in higher eukaryotes: two enzymes are present in potato mitochondria. Plant J. 20, 79-87
    • (1999) Plant J. , vol.20 , pp. 79-87
    • Rasmusson, A.G.1    Svensson, A.S.2    Knoop, V.3    Grohmann, L.4    Brennicke, A.5
  • 37
  • 38
    • 0032425311 scopus 로고    scopus 로고
    • The internal rotenone-insensitive NADPH dehydrogenase contributes to malate oxidation by potato tuber and pea leaf mitochondria
    • Agius, S. C., Bykova, N. V., Igamberdiev, A. U. and Møller, I. M. (1998) The internal rotenone-insensitive NADPH dehydrogenase contributes to malate oxidation by potato tuber and pea leaf mitochondria. Physiol. Plant. 104, 329-336
    • (1998) Physiol. Plant. , vol.104 , pp. 329-336
    • Agius, S.C.1    Bykova, N.V.2    Igamberdiev, A.U.3    Møller, I.M.4
  • 39
    • 0038070088 scopus 로고    scopus 로고
    • Investigation of the role and mechanism of IF1 and STF1 proteins, twin inhibitory peptides which interact with the yeast mitochondrial ATP synthase
    • Venard, R., Brèthes, D., Giraud, M. F., Vaillier, J., Velours, J. and Haraux, F. (2003) Investigation of the role and mechanism of IF1 and STF1 proteins, twin inhibitory peptides which interact with the yeast mitochondrial ATP synthase. Biochemistry 42, 7626-7636
    • (2003) Biochemistry , vol.42 , pp. 7626-7636
    • Venard, R.1    Brèthes, D.2    Giraud, M.F.3    Vaillier, J.4    Velours, J.5    Haraux, F.6
  • 40
    • 0019586951 scopus 로고
    • Purification of NAD malic enzyme from potato and investigation of some physical and kinetic properties
    • Grover, S. D., Canellas, P. F. and Wedding, R. T. (1981) Purification of NAD malic enzyme from potato and investigation of some physical and kinetic properties. Arch. Biochem. Biophys. 209, 396-407
    • (1981) Arch. Biochem. Biophys. , vol.209 , pp. 396-407
    • Grover, S.D.1    Canellas, P.F.2    Wedding, R.T.3
  • 41
    • 0014409086 scopus 로고
    • Kinetic studies on the mechanism of the malate dehydrogenase reaction
    • Heyde, E. and Ainsworth, S. (1968) Kinetic studies on the mechanism of the malate dehydrogenase reaction. J. Biol. Chem. 243, 2413-2423
    • (1968) J. Biol. Chem. , vol.243 , pp. 2413-2423
    • Heyde, E.1    Ainsworth, S.2
  • 42


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.