메뉴 건너뛰기




Volumn 47, Issue 34, 2008, Pages 8894-8901

The iron-sulfur cluster of electron transfer flavoprotein-ubiquinone oxidoreductase is the electron acceptor for electron transfer flavoprotein

Author keywords

[No Author keywords available]

Indexed keywords

CHLORINE COMPOUNDS; ELECTRON TRANSITIONS; ENZYMES; SULFUR;

EID: 50149109392     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi800507p     Document Type: Article
Times cited : (24)

References (26)
  • 1
    • 0017691203 scopus 로고
    • A new iron-sulfur protein of the respiratory chain: A component of the fatty acid oxidation pathway
    • Ruzicka, F. J., and Beinert, H. (1977) A new iron-sulfur protein of the respiratory chain: a component of the fatty acid oxidation pathway. J. Biol. Chem. 252, 8440-8445.
    • (1977) J. Biol. Chem , vol.252 , pp. 8440-8445
    • Ruzicka, F.J.1    Beinert, H.2
  • 2
    • 35448974949 scopus 로고    scopus 로고
    • Dynamics driving function - new insights from electron transferring flavoproteins and partner complexes
    • Toogood, H. S., Leys, D., and Scrutton, N. S. (2007) Dynamics driving function - new insights from electron transferring flavoproteins and partner complexes. FEBS J. 274, 5481-5504.
    • (2007) FEBS J , vol.274 , pp. 5481-5504
    • Toogood, H.S.1    Leys, D.2    Scrutton, N.S.3
  • 3
    • 0036396930 scopus 로고    scopus 로고
    • Glutaric acidemia type II: Gene structure and mutations of the electron transfer flavoprotein ubiquinone oxidoreductase (ETF-QO) gene
    • Goodman, S. I., Binard, R. J., Woontner, M. R., and Frerman, F. E. (2002) Glutaric acidemia type II: gene structure and mutations of the electron transfer flavoprotein ubiquinone oxidoreductase (ETF-QO) gene. Mol. Genet. Metab. 77, 86-90.
    • (2002) Mol. Genet. Metab , vol.77 , pp. 86-90
    • Goodman, S.I.1    Binard, R.J.2    Woontner, M.R.3    Frerman, F.E.4
  • 4
    • 33645967816 scopus 로고    scopus 로고
    • So doctor, what exactly is wrong with my muscles? Glutaric aciduria type II presenting in a teenager
    • Beresford, M. W., Pourfarzam, M., Turnbull, D. M., and Davidson, J. E. (2006) So doctor, what exactly is wrong with my muscles? Glutaric aciduria type II presenting in a teenager. Neuromuscular Disord. 16, 269-273.
    • (2006) Neuromuscular Disord , vol.16 , pp. 269-273
    • Beresford, M.W.1    Pourfarzam, M.2    Turnbull, D.M.3    Davidson, J.E.4
  • 5
    • 33750814320 scopus 로고    scopus 로고
    • Structure of electron transfer flavoprotein ubiquinone oxidoreductase and electron transfer to the mitochondrial ubuiquinone pool
    • Zhang, J., Frerman, F. E., and Kim, J.-J. (2006) Structure of electron transfer flavoprotein ubiquinone oxidoreductase and electron transfer to the mitochondrial ubuiquinone pool. Proc. Natl. Acad. Sci. U.S.A. 103, 16212-16217.
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 16212-16217
    • Zhang, J.1    Frerman, F.E.2    Kim, J.-J.3
  • 6
    • 0033523919 scopus 로고    scopus 로고
    • Natural engineering principals of electron tunnelling in biological oxidation-reduction
    • Page, C. C., Moser, C. C., Chen, X., and Dutton, P. L. (1999) Natural engineering principals of electron tunnelling in biological oxidation-reduction. Nature 402, 47-52.
    • (1999) Nature , vol.402 , pp. 47-52
    • Page, C.C.1    Moser, C.C.2    Chen, X.3    Dutton, P.L.4
  • 7
    • 0022706389 scopus 로고
    • The relation between the divergence of sequence and structure in proteins
    • Chothia, C., and Lesk, A. M. (1986) The relation between the divergence of sequence and structure in proteins. EMBO J. 5, 823-826.
    • (1986) EMBO J , vol.5 , pp. 823-826
    • Chothia, C.1    Lesk, A.M.2
  • 9
    • 0000452846 scopus 로고
    • Model systems for flavoenzyme activity. Stabilization of the flavin radical anion through specific hydrogen bond interactions
    • Breinlinger, E., Niemz, A., and Rotello, V. M. (1995) Model systems for flavoenzyme activity. Stabilization of the flavin radical anion through specific hydrogen bond interactions. J. Am. Chem. Soc. 117, 5379-5380.
    • (1995) J. Am. Chem. Soc , vol.117 , pp. 5379-5380
    • Breinlinger, E.1    Niemz, A.2    Rotello, V.M.3
  • 10
    • 0030593468 scopus 로고    scopus 로고
    • Overproduction of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • Miroux, B., and Walker, J. E. (1996) Overproduction of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J. Mol. Biol. 260, 289-298.
    • (1996) J. Mol. Biol , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 11
    • 0037117756 scopus 로고    scopus 로고
    • Characterization of an iron-sulfur cluster assembly protein (ISU1) from Schizosaccharomyces pombe
    • Wu, G., Mansey, S. S., Wu, S., Suresus, K. K., Foster, M. W., and Cowan, J. A. (2002) Characterization of an iron-sulfur cluster assembly protein (ISU1) from Schizosaccharomyces pombe. Biochemistry 41, 5024-5032.
    • (2002) Biochemistry , vol.41 , pp. 5024-5032
    • Wu, G.1    Mansey, S.S.2    Wu, S.3    Suresus, K.K.4    Foster, M.W.5    Cowan, J.A.6
  • 12
    • 0018067152 scopus 로고
    • Quantitative determination of noncovalently bound flavins: Types and methods of analysis
    • Siegel, L. M. (1978) Quantitative determination of noncovalently bound flavins: types and methods of analysis. Methods Enzymol. 53, 419-429.
    • (1978) Methods Enzymol , vol.53 , pp. 419-429
    • Siegel, L.M.1
  • 13
    • 0023283867 scopus 로고
    • Reactions of electron transfer flavoprotein and electron transfer flavoprotein-ubiquinone oxidoreductase
    • Ramsay, R. R., Steenkamp, D. J., and Husain, M. (1987) Reactions of electron transfer flavoprotein and electron transfer flavoprotein-ubiquinone oxidoreductase. Biochem. J. 241, 883-892.
    • (1987) Biochem. J , vol.241 , pp. 883-892
    • Ramsay, R.R.1    Steenkamp, D.J.2    Husain, M.3
  • 14
    • 0022347073 scopus 로고
    • Electron transfer flavoprotein-ubiquinone oxidoreductase from pig liver: Purification and molecular, redox and catalytic properties
    • Beckmann, J. D., and Frerman, F. E. (1985) Electron transfer flavoprotein-ubiquinone oxidoreductase from pig liver: purification and molecular, redox and catalytic properties. Biochemistry 24, 3913-3921.
    • (1985) Biochemistry , vol.24 , pp. 3913-3921
    • Beckmann, J.D.1    Frerman, F.E.2
  • 16
    • 0034669323 scopus 로고    scopus 로고
    • The use of protocatechuate dioxygenase for maintaining anaerobic conditions in biochemical experiments
    • Patil, P. V., and Ballou, D. P. (2000) The use of protocatechuate dioxygenase for maintaining anaerobic conditions in biochemical experiments. Anal. Biochem. 286, 187-192.
    • (2000) Anal. Biochem , vol.286 , pp. 187-192
    • Patil, P.V.1    Ballou, D.P.2
  • 17
    • 0018115502 scopus 로고
    • Redox potentiomery: Determination of mid-point potentials of oxidation reduction components of biological electron transfer systems
    • Dutton, P. L. (1978) Redox potentiomery: determination of mid-point potentials of oxidation reduction components of biological electron transfer systems. Methods Enzymol. 54, 411-435.
    • (1978) Methods Enzymol , vol.54 , pp. 411-435
    • Dutton, P.L.1
  • 18
    • 38149013941 scopus 로고    scopus 로고
    • Electron Paramagnetic Resonance Characterization and Interspin Distance Measurement of Electron Transfer Flavoprotein Ubiquinone Oxidoreductase (ETF-QO)
    • Fielding, A. J., Usselman, R. J., Watmough, N., Simkovic, M., Frerman, F. E., Eaton, G. R., and Eaton, G. R. (2008) Electron Paramagnetic Resonance Characterization and Interspin Distance Measurement of Electron Transfer Flavoprotein Ubiquinone Oxidoreductase (ETF-QO). J. Magn. Reson. 190, 222-232.
    • (2008) J. Magn. Reson , vol.190 , pp. 222-232
    • Fielding, A.J.1    Usselman, R.J.2    Watmough, N.3    Simkovic, M.4    Frerman, F.E.5    Eaton, G.R.6    Eaton, G.R.7
  • 20
    • 0000852119 scopus 로고
    • Time-Domain Electron Paramagnetic Resonance as a Probe of Electron-Electron Spin-Spin Interaction in Spin-Labeled Low-Spin Iron Porphyrins
    • Rakowsky, M. H., More, K. M., Kulikov, A. V., Eaton, G. R., and Eaton, S. S. (1995) Time-Domain Electron Paramagnetic Resonance as a Probe of Electron-Electron Spin-Spin Interaction in Spin-Labeled Low-Spin Iron Porphyrins. J. Am. Chem. Soc. 117, 2049-2057.
    • (1995) J. Am. Chem. Soc , vol.117 , pp. 2049-2057
    • Rakowsky, M.H.1    More, K.M.2    Kulikov, A.V.3    Eaton, G.R.4    Eaton, S.S.5
  • 21
    • 0026448652 scopus 로고
    • Redox properties of electron-transfer flavoprotein ubiquinone oxidoreductase as determined by EPR-spectroelectrochemistry
    • Paulsen, K. E., Orville, A. M., Frerman, F. E., Lipscomb, J. D., and Stankovich, M. T. (1992) Redox properties of electron-transfer flavoprotein ubiquinone oxidoreductase as determined by EPR-spectroelectrochemistry. Biochemistry 31, 11755-11761.
    • (1992) Biochemistry , vol.31 , pp. 11755-11761
    • Paulsen, K.E.1    Orville, A.M.2    Frerman, F.E.3    Lipscomb, J.D.4    Stankovich, M.T.5
  • 22
    • 0001773735 scopus 로고    scopus 로고
    • Relaxation times of organic radicals and transition metal ions
    • Eaton, S. S., and Eaton, G. R. (2000) Relaxation times of organic radicals and transition metal ions. Biol. Magn. Reson. 19, 29-154.
    • (2000) Biol. Magn. Reson , vol.19 , pp. 29-154
    • Eaton, S.S.1    Eaton, G.R.2
  • 24
    • 0031010679 scopus 로고    scopus 로고
    • Flavin mononucleotide-binding domain of the flavoprotein component of the sulfite reductase from Escherichia coli
    • Coves, J., Zeghouf, M., Macherel, D., Guigliarelli, B., Asso, M., and Fontecave, M. (1997) Flavin mononucleotide-binding domain of the flavoprotein component of the sulfite reductase from Escherichia coli. Biochemistry 36, 5921-5928.
    • (1997) Biochemistry , vol.36 , pp. 5921-5928
    • Coves, J.1    Zeghouf, M.2    Macherel, D.3    Guigliarelli, B.4    Asso, M.5    Fontecave, M.6
  • 25
    • 0037097010 scopus 로고    scopus 로고
    • Expression of human electron transfer flavoprotein-ubiquinone oxidoreductase from a baculovirus vector: Kinetic and spectral characterization of the human protein
    • Simkovic, M., Degala, G. D., Eaton, S. S., and Frerman, F. E. (2002) Expression of human electron transfer flavoprotein-ubiquinone oxidoreductase from a baculovirus vector: kinetic and spectral characterization of the human protein. Biochem. J. 364, 659-667.
    • (2002) Biochem. J , vol.364 , pp. 659-667
    • Simkovic, M.1    Degala, G.D.2    Eaton, S.S.3    Frerman, F.E.4
  • 26
    • 33750814320 scopus 로고    scopus 로고
    • Structure of electron transfer flavoprotein ubiquinone oxidoreductase and electron transfer to the mitochondrial ubuiquinone pool
    • Zhang, J., Frerman, F. E., and Kim, J.-J. (2006) Structure of electron transfer flavoprotein ubiquinone oxidoreductase and electron transfer to the mitochondrial ubuiquinone pool. Proc. Natl. Acad. Sci. U.S.A. 103, 16212-16217.
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 16212-16217
    • Zhang, J.1    Frerman, F.E.2    Kim, J.-J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.