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Volumn 40, Issue 5, 2013, Pages 429-434

Characteristics of functioning of succinate dehydrogenase from flight muscles of the bumblebee Bombus terrestris (L.)

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EID: 84884197172     PISSN: 10623590     EISSN: None     Source Type: Journal    
DOI: 10.1134/S1062359013050051     Document Type: Article
Times cited : (4)

References (40)
  • 1
    • 0019320925 scopus 로고
    • Peptides from complex II active in reconstitution of succinate ubiquinone reductase
    • Ackrell, B. A., Ball, M. B., and Kearney, E. B., Peptides from complex II active in reconstitution of succinate ubiquinone reductase, J. Biol. Chem., 1980, vol. 255, pp. 2761-2769.
    • (1980) J. Biol. Chem. , vol.255 , pp. 2761-2769
    • Ackrell, B.A.1    Ball, M.B.2    Kearney, E.B.3
  • 2
    • 12844262009 scopus 로고    scopus 로고
    • Isolation and properties of cytoplasmic alpha-glycerol 3-phosphate dehydrogenase from the pectoral muscle of the fruit bat Eidolon helvum
    • Agboola, F. K., Thomson, A., and Afolayan, A., Isolation and properties of cytoplasmic alpha-glycerol 3-phosphate dehydrogenase from the pectoral muscle of the fruit bat Eidolon helvum, J. Biochem. Mol. Biol., 2003, vol. 36, pp. 159-166.
    • (2003) J. Biochem. Mol. Biol. , vol.36 , pp. 159-166
    • Agboola, F.K.1    Thomson, A.2    Afolayan, A.3
  • 3
    • 36348999715 scopus 로고    scopus 로고
    • Tricarboxylic acid cycle intermediate pool size functional importance for oxidative metabolism in exercising human skeletal muscle
    • Bowtell, J. L., Marwood, S., Bruce, M., et al., Tricarboxylic acid cycle intermediate pool size functional importance for oxidative metabolism in exercising human skeletal muscle, Sports Med., 2007, vol. 37, pp. 1071-1088.
    • (2007) Sports Med. , vol.37 , pp. 1071-1088
    • Bowtell, J.L.1    Marwood, S.2    Bruce, M.3
  • 4
    • 0342597207 scopus 로고
    • Succinate dehydrogenase. A partial purification from mung bean hypocotils and soybean cotiledons
    • Burke, J. J., Siedow, J. N., and Moreland, D. E., Succinate dehydrogenase. A partial purification from mung bean hypocotils and soybean cotiledons, Plant. Physiol., 1982, vol. 70, pp. 1577-1581.
    • (1982) Plant. Physiol. , vol.70 , pp. 1577-1581
    • Burke, J.J.1    Siedow, J.N.2    Moreland, D.E.3
  • 5
    • 77249105402 scopus 로고    scopus 로고
    • The alpha glycerophosphate cycle in Drosophila melanogaster. VI. Structure and evolution of enzyme paralogs in the genus Drosophila
    • Carmon, A. and MacIntyre, R., The alpha glycerophosphate cycle in Drosophila melanogaster. VI. Structure and evolution of enzyme paralogs in the genus Drosophila, J. Hered., 2010, vol. 101, pp. 225-234.
    • (2010) J. Hered. , vol.101 , pp. 225-234
    • Carmon, A.1    MacIntyre, R.2
  • 6
    • 49849113731 scopus 로고
    • Succinic acid dehydrogenase activity in the gill epithelium of euryhaline fishes
    • Conte, G. P. and Tripp, M. S., Succinic acid dehydrogenase activity in the gill epithelium of euryhaline fishes, Int. J. Biochem., 1970, vol. 1, pp. 129-138.
    • (1970) Int. J. Biochem. , vol.1 , pp. 129-138
    • Conte, G.P.1    Tripp, M.S.2
  • 7
    • 0017077162 scopus 로고
    • Accelerated catalysis by active succinate dehydrogenase: a refection of a novel regulatory site
    • Cooper, A. and Gutman, M., Accelerated catalysis by active succinate dehydrogenase: a refection of a novel regulatory site, FEBS Lett., 1976, vol. 67, pp. 130-133.
    • (1976) FEBS Lett. , vol.67 , pp. 130-133
    • Cooper, A.1    Gutman, M.2
  • 9
    • 78651153791 scopus 로고
    • Disc electrophoresis. Method and application to human serum proteins
    • Davis, B. J., Disc electrophoresis. Method and application to human serum proteins, Ann. N. Y. Acad. Sci., 1964, vol. 121, pp. 404-427.
    • (1964) Ann. N.Y. Acad. Sci. , vol.121 , pp. 404-427
    • Davis, B.J.1
  • 11
    • 33744478401 scopus 로고    scopus 로고
    • Free radical theory of aging: an update: increasing the functional life span
    • Harman, D. A., Free radical theory of aging: an update: increasing the functional life span, Ann. N. Y. Acad. Sci., 2006, vol. 1067, pp. 10-21.
    • (2006) Ann. N.Y. Acad. Sci. , vol.1067 , pp. 10-21
    • Harman, D.A.1
  • 12
    • 3843127672 scopus 로고
    • The presence of two forms of succinate dehydrogenase in sweet potato roots mitochondria
    • Hattori, T. and Asahi, T., The presence of two forms of succinate dehydrogenase in sweet potato roots mitochondria, Plant Cell Physiol., 1982, vol. 23, pp. 515-523.
    • (1982) Plant Cell Physiol. , vol.23 , pp. 515-523
    • Hattori, T.1    Asahi, T.2
  • 13
    • 7144219831 scopus 로고
    • Isolation and characterization of the succinate dehydrogenase complex of plant mitochondria
    • Igamberdiev, A. U. and Falaleeva, M. I., Isolation and characterization of the succinate dehydrogenase complex of plant mitochondria, Biokhimiya, 1994, no. 8, pp. 895-900.
    • (1994) Biokhimiya , pp. 895-900
    • Igamberdiev, A.U.1    Falaleeva, M.I.2
  • 14
    • 84875711829 scopus 로고    scopus 로고
    • Catalytic mechanisms of complex II enzymes: a structural perspective
    • Iverson, T. M., Catalytic mechanisms of complex II enzymes: a structural perspective, Biochim. Biophys. Acta, 2012, vol. 1827, no. 5, pp. 648-657.
    • (2012) Biochim. Biophys. Acta , vol.1827 , Issue.5 , pp. 648-657
    • Iverson, T.M.1
  • 15
    • 0016364673 scopus 로고
    • Activation of succinate dehydrogenase by anions and pH
    • Kearney, E. B., Ackrell, B. A. C., Mayr, M., and Singer, T. P., Activation of succinate dehydrogenase by anions and pH, J. Biol. Chem., 1974, vol. 249, pp. 2016-2020.
    • (1974) J. Biol. Chem. , vol.249 , pp. 2016-2020
    • Kearney, E.B.1    Ackrell, B.A.C.2    Mayr, M.3    Singer, T.P.4
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmly, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature, 1970, vol. 77, pp. 680-683.
    • (1970) Nature , vol.77 , pp. 680-683
    • Laemmly, U.K.1
  • 20
    • 77949634569 scopus 로고    scopus 로고
    • Structure and organization of mitochondrial respiratory complexes: a new understanding of an old subject
    • Lenaz, G. and Genova, M. L., Structure and organization of mitochondrial respiratory complexes: a new understanding of an old subject, Antioxid. Redox Signal., 2010, vol. 12, pp. 961-1008.
    • (2010) Antioxid. Redox Signal. , vol.12 , pp. 961-1008
    • Lenaz, G.1    Genova, M.L.2
  • 21
    • 71849104860 scopus 로고
    • Protein measurement with the folin phenol reagent
    • Lowry, T., Protein measurement with the folin phenol reagent, J. Biol. Chem., 1951, vol. 193, pp. 265-275.
    • (1951) J. Biol. Chem. , vol.193 , pp. 265-275
    • Lowry, T.1
  • 23
    • 24344508510 scopus 로고    scopus 로고
    • The topology of superoxide production by complex III and glycerol 3-phosphate dehydrogenase in Drosophilla mitochondria
    • Miwa, S. and Brand, M. D., The topology of superoxide production by complex III and glycerol 3-phosphate dehydrogenase in Drosophilla mitochondria, Biochim. Biophys. Acta, 2005, vol. 1709, pp. 214-219.
    • (2005) Biochim. Biophys. Acta , vol.1709 , pp. 214-219
    • Miwa, S.1    Brand, M.D.2
  • 24
    • 0026079737 scopus 로고
    • Purification and characterization of an archaebacterial succinate dehydrogenase complex from the plasma membrane of the thermoacidophile Sulfolobus acidocaldarius
    • Moll, R. and Schafer, G., Purification and characterization of an archaebacterial succinate dehydrogenase complex from the plasma membrane of the thermoacidophile Sulfolobus acidocaldarius, Eur. J. Biochem., 1991, vol. 201, pp. 593-600.
    • (1991) Eur. J. Biochem. , vol.201 , pp. 593-600
    • Moll, R.1    Schafer, G.2
  • 25
    • 84872102687 scopus 로고    scopus 로고
    • The function and the role of the mitochondrial glycerol-3-phosphate dehydrogenase in mammalian tissues
    • Mráček, T., Drahota, Z., and Houštěk, L., The function and the role of the mitochondrial glycerol-3-phosphate dehydrogenase in mammalian tissues, Biochim. Biophys. Acta, 2013. doi: 10. 1016/j. bbabio. 2012. 11. 014.
    • (2013) Biochim. Biophys. Acta
    • Mráček, T.1    Drahota, Z.2    Houštěk, L.3
  • 26
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • Murphy, M. P., How mitochondria produce reactive oxygen species, Biochem. J., 2009, vol. 417, pp. 1-13.
    • (2009) Biochem. J. , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 27
    • 84871139444 scopus 로고    scopus 로고
    • A refined analysis of superoxide production by mitochondrial sn-glycerol 3-phosphate dehydrogenase
    • Orr, A. L., Quinlan, C. L., Perevoshchikova, I. V., and Brand, M. D., A refined analysis of superoxide production by mitochondrial sn-glycerol 3-phosphate dehydrogenase, J. Biol. Chem., 2012, vol. 287, pp. 42921-42935.
    • (2012) J. Biol. Chem. , vol.287 , pp. 42921-42935
    • Orr, A.L.1    Quinlan, C.L.2    Perevoshchikova, I.V.3    Brand, M.D.4
  • 28
    • 77952885778 scopus 로고    scopus 로고
    • Succinate dehydrogenase-assembly, regulation and role in human disease
    • Rutter, J., Winge, D. R., and Schiffman, J. D., Succinate dehydrogenase-assembly, regulation and role in human disease, Mitochondrion, 2010, vol. 10, pp. 393-401.
    • (2010) Mitochondrion , vol.10 , pp. 393-401
    • Rutter, J.1    Winge, D.R.2    Schiffman, J.D.3
  • 30
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O., and Mann, M., Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels, Anal. Chem., 1996, vol. 68, pp. 850-858.
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 31
    • 50449116414 scopus 로고
    • Solubilization assay and purification of succinate dehydrogenase
    • Singer, T. P. and Kearney, E. B., Solubilization assay and purification of succinate dehydrogenase, Biochem. Biophys. Acta, 1954, vol. 15, pp. 151-153.
    • (1954) Biochem. Biophys. Acta , vol.15 , pp. 151-153
    • Singer, T.P.1    Kearney, E.B.2
  • 32
    • 57649233079 scopus 로고    scopus 로고
    • The role of mitochondria in reactive oxygen species metabolism and signaling
    • Starkov, A. A., The role of mitochondria in reactive oxygen species metabolism and signaling, Ann. N. Y. Acad. Sci., 2008, vol. 1147, pp. 37-52.
    • (2008) Ann. N.Y. Acad. Sci. , vol.1147 , pp. 37-52
    • Starkov, A.A.1
  • 33
    • 0029861414 scopus 로고    scopus 로고
    • Energy metabolism, enzymatic flux capacities, and metabolic flux rates in flying honeybees
    • Suarez, R. K., Lightont, J. R., Joost, B., et al., Energy metabolism, enzymatic flux capacities, and metabolic flux rates in flying honeybees, Physiology, 1996, vol. 93, pp. 12616-12620.
    • (1996) Physiology , vol.93 , pp. 12616-12620
    • Suarez, R.K.1    Lightont, J.R.2    Joost, B.3
  • 34
    • 0034494266 scopus 로고    scopus 로고
    • Energy metabolism during insect flight: biochemical design and physiological performance
    • Suarez, R. K., Energy metabolism during insect flight: biochemical design and physiological performance, Physiol. Biochem. Zool., 2000, vol. 73, pp. 765-771.
    • (2000) Physiol. Biochem. Zool. , vol.73 , pp. 765-771
    • Suarez, R.K.1
  • 35
    • 26844465441 scopus 로고    scopus 로고
    • Energy metabolism in orchid bee flight muscles: carbohydrate fuels all
    • Suarez, R. K., Darveau, C. A., and Welch, K. C., Energy metabolism in orchid bee flight muscles: carbohydrate fuels all, J. Exper. Biol., 2005, vol. 208, pp. 3573-3579.
    • (2005) J. Exper. Biol. , vol.208 , pp. 3573-3579
    • Suarez, R.K.1    Darveau, C.A.2    Welch, K.C.3
  • 36
    • 0033978797 scopus 로고    scopus 로고
    • Purification and characterization of plasmodium falciparum succinate dehydrogenase
    • Suraveratum, N., Krungkrai, S. R., Leangaramgul, P., et al., Purification and characterization of plasmodium falciparum succinate dehydrogenase, Mol. Biochem. Parasitol., 2000, vol. 105, pp. 215-222.
    • (2000) Mol. Biochem. Parasitol. , vol.105 , pp. 215-222
    • Suraveratum, N.1    Krungkrai, S.R.2    Leangaramgul, P.3
  • 37
    • 0022991835 scopus 로고
    • Succinate ubiquinol reductase component of the respiratory chain
    • Vinogradov, A. D., Succinate ubiquinol reductase component of the respiratory chain, Biokhimiya, 1986, no. 12, pp. 1944-1973.
    • (1986) Biokhimiya , pp. 1944-1973
    • Vinogradov, A.D.1
  • 38
    • 42149117451 scopus 로고    scopus 로고
    • Structure of glycerol-3-phosphate dehydrogenase, an essential monotopic membrane enzyme involved in respiration and metabolism
    • Yeh, J. I., Chinte, U., and Du, S., Structure of glycerol-3-phosphate dehydrogenase, an essential monotopic membrane enzyme involved in respiration and metabolism, Proc. Natl. Acad. Sci. USA, 2008, vol. 105, pp. 3280-3285.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 3280-3285
    • Yeh, J.I.1    Chinte, U.2    Du, S.3
  • 39
    • 0027310147 scopus 로고
    • Mitochondrial ubiquinol-cytochrome c reductase complex: crystallization and protein: ubiquinone interaction
    • Yu, C. A. and Yu, L., Mitochondrial ubiquinol-cytochrome c reductase complex: crystallization and protein: ubiquinone interaction, J. Bioenerg. Biomembr., 1993, vol. 25, pp. 259-273.
    • (1993) J. Bioenerg. Biomembr. , vol.25 , pp. 259-273
    • Yu, C.A.1    Yu, L.2
  • 40
    • 84870698437 scopus 로고    scopus 로고
    • Burst of succinate dehydrogenase and α-ketoglutarate dehydrogenase activity in concert with the expression of genes coding for respiratory chain proteins underlies short-term beneficial physiological stress in mitochondria
    • Zakharchenko, M. V., Zakharchenko, A. V., Khunderyakova, N. V., et al., Burst of succinate dehydrogenase and α-ketoglutarate dehydrogenase activity in concert with the expression of genes coding for respiratory chain proteins underlies short-term beneficial physiological stress in mitochondria, Int. J. Biochem. Cell Biol., 2013, vol. 45, pp. 190-200.
    • (2013) Int. J. Biochem. Cell Biol. , vol.45 , pp. 190-200
    • Zakharchenko, M.V.1    Zakharchenko, A.V.2    Khunderyakova, N.V.3


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