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Volumn 20, Issue 3, 2011, Pages 610-620

Electron transfer flavoprotein domain II orientation monitored using double electron-electron resonance between an enzymatically reduced, native FAD cofactor, and spin labels

Author keywords

Double electron electron resonance; FAD semiquinone; Interspin distance; Molecular dynamics simulation; Q band DEER

Indexed keywords

ELECTRON TRANSFERRING FLAVOPROTEIN; FLAVINE ADENINE NUCLEOTIDE; HETERODIMER; MEDIUM CHAIN ACYL COENZYME A DEHYDROGENASE; OXIDOREDUCTASE;

EID: 79952170325     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.595     Document Type: Article
Times cited : (11)

References (41)
  • 1
    • 0029118352 scopus 로고
    • High level expression of an altered cDNA encoding human isovaleryl-CoA dehydrogenase in Escherichia coli
    • Al-Walid A-W, Vockley J (1995) High level expression of an altered cDNA encoding human isovaleryl-CoA dehydrogenase in Escherichia coli. Gene 160:263-267.
    • (1995) Gene , vol.160 , pp. 263-267
    • Al-Walid, A.-W.1    Vockley, J.2
  • 2
    • 0031952564 scopus 로고    scopus 로고
    • Identification of the catalytic residue of human short/branched chain acyl-CoA dehydrogenase by in vitro mutagenesis
    • DOI 10.1016/S0167-4838(97)00161-1, PII S0167483897001611
    • Binzak B, Willard J, Vockley J (1998) Identification of the catalytic residue of human short/branched chain acyl-CoA dehydrogenate by in vitro mutagenesis. Biochim Biophys Acta 1382:137-142. (Pubitemid 28122943)
    • (1998) Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology , vol.1382 , Issue.1 , pp. 137-142
    • Binzak, B.1    Willard, J.2    Vockley, J.3
  • 3
    • 0034687154 scopus 로고    scopus 로고
    • Proton abstraction reaction, steady state kinetics and oxidation-reduction potential of human glutaryl-CoA dehydrogenase
    • Dwyer TM, Rao KS, Goodman SI, Frerman FE (2000) Proton abstraction reaction, steady state kinetics and oxidation-reduction potential of human glutaryl-CoA dehydrogenase. Biochemistry 39:11488-11499.
    • (2000) Biochemistry , vol.39 , pp. 11488-11499
    • Dwyer, T.M.1    Rao, K.S.2    Goodman, S.I.3    Frerman, F.E.4
  • 5
    • 0017691203 scopus 로고
    • A new iron sulfur flavoprotein of the respiratory chain. A component of the fatty acid beta oxidation pathway
    • Ruzicka FJ, 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. (Pubitemid 8243718)
    • (1977) Journal of Biological Chemistry , vol.252 , Issue.23 , pp. 8440-8445
    • Ruzicka, F.J.1    Beinert, H.2
  • 6
    • 35448974949 scopus 로고    scopus 로고
    • Dynamics driving function - New insights from electron transferring flavoproteins and partner complexes
    • DOI 10.1111/j.1742-4658.2007.06107.x
    • Toogood HS, Leys D, Scrutton NS (2007) Dynamics driving function - new insights from electron transferring flavoproteins and partner complexes. FEBS J 274:5481-5504. (Pubitemid 47622089)
    • (2007) FEBS Journal , vol.274 , Issue.21 , pp. 5481-5504
    • Toogood, H.S.1    Leys, D.2    Scrutton, N.S.3
  • 8
    • 50149109392 scopus 로고    scopus 로고
    • The Iron-Sulfur Cluster of Electron Transfer Flavoprotein-ubiquinone Oxidoreductase (ETF-QO) is the Electron Acceptor for Electron Transfer Flavoprotein
    • Swanson MA, Usselman RJ, Frerman FE, Eaton GR, Eaton SS (2008) The Iron-Sulfur Cluster of Electron Transfer Flavoprotein-ubiquinone Oxidoreductase (ETF-QO) is the Electron Acceptor for Electron Transfer Flavoprotein. Biochemistry 47:8894-8901.
    • (2008) Biochemistry , vol.47 , pp. 8894-8901
    • Swanson, M.A.1    Usselman, R.J.2    Frerman, F.E.3    Eaton, G.R.4    Eaton, S.S.5
  • 9
    • 0036396930 scopus 로고    scopus 로고
    • Glutaric acidemia type II: Gene structure and mutations of the electron transfer flavoprotein:ubiquinone oxidoreductase (ETF:QO) gene
    • DOI 10.1016/S1096-7192(02)00138-5, PII S1096719202001385
    • Goodman SI, Binard RJ, Woontner MR, Frerman FE (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. (Pubitemid 35178519)
    • (2002) Molecular Genetics and Metabolism , vol.77 , Issue.1-2 , pp. 86-90
    • Goodman, S.I.1    Binard, R.J.2    Woontner, M.R.3    Frerman, F.E.4
  • 10
    • 33748571891 scopus 로고    scopus 로고
    • So doctor, what exactly is wrong with my muscles? Glutaric aciduria type II presenting in a teenager
    • Beresford MW, Pourfarzam M, Turnbull DM, Davidson JE (2006) So doctor, what exactly is wrong with my muscles? Glutaric aciduria type II presenting in a teenager. Neuromuscular Disorders 16:269-273.
    • (2006) Neuromuscular Disorders , vol.16 , pp. 269-273
    • Beresford, M.W.1    Pourfarzam, M.2    Turnbull, D.M.3    Davidson, J.E.4
  • 11
    • 0033573853 scopus 로고    scopus 로고
    • Crystal structure of Paracoccus denitrificans electron transfer flavoprotein: Structural and electrostatic analysis of a conserved flavin binding domain
    • Roberts DL, Salazar D, Fulmer JP, Frerman FE, and Kim J-JP (1999) Crystal structure of Paracoccus denitrificans electron transfer flavoprotein: structural and electrostatic analysis of a conserved flavin binding domain. Biochemistry 38:1977-1989.
    • (1999) Biochemistry , vol.38 , pp. 1977-1989
    • Roberts, D.L.1    Salazar, D.2    Fulmer, J.P.3    Frerman, F.E.4    Kim, J.-J.P.5
  • 13
    • 3543004682 scopus 로고    scopus 로고
    • Extensive domain motion and electron transfer in the human electron transferring flavoproteinmedium chain acyl-CoA dehydrogenase complex
    • DOI 10.1074/jbc.M404884200
    • Toogood HS, van Thiel A, Basran J, Sutcliffe MJ, Scrutton NS, Leys D. (2004) Extensive Domain Motion and Electron Transfer in the Human Electron Transferring Protein Medium Chain Acyl-CoA Dehydrogenase Complex. J Biol Chem 279:32904-32912. (Pubitemid 39014750)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.31 , pp. 32904-32912
    • Toogood, H.S.1    Van, T.A.2    Basran, J.3    Sutcliffe, M.J.4    Scrutton, N.S.5    Leys, D.6
  • 14
    • 0142231009 scopus 로고    scopus 로고
    • Mechanism for electron transfer within and between proteins
    • Page CC, Moser CC, Dutton PL (2003) Mechanism for electron transfer within and between proteins. Curr Opin Chem Biol 7:55-116.
    • (2003) Curr Opin Chem Biol , vol.7 , pp. 55-116
    • Page, C.C.1    Moser, C.C.2    Dutton, P.L.3
  • 15
    • 24044466133 scopus 로고    scopus 로고
    • Stabilization of non-productive conformations underpins rapid electron transfer to electron-transferring flavoprotein
    • DOI 10.1074/jbc.M505562200
    • Toogood HS, van Thiel A, Scrutton NS, Leys D (2005) Stabilization of Non-productive Conformations Underpins Rapid Electron Transfer to Electron-transferring Flavoprotein. J Biol Chem 280:30361-30366. (Pubitemid 41216218)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.34 , pp. 30361-30366
    • Toogood, H.S.1    Van, T.A.2    Scrutton, N.S.3    Leys, D.4
  • 16
    • 0026525317 scopus 로고
    • Structural and redox relationships between Paracoccus denitrificans, porcine, and human electron-transferring flavoproteins
    • Watmough N, Kiss J, Frerman FE (1992) Structural and redox relationships between Paracoccus denitrificans, porcine, and human electron-transferring flavoproteins. Eur J Biochem 205:1089-1097.
    • (1992) Eur J Biochem , vol.205 , pp. 1089-1097
    • Watmough, N.1    Kiss, J.2    Frerman, F.E.3
  • 17
    • 70450193175 scopus 로고    scopus 로고
    • DEER Distance Measurement between a Spin Label and a Native FAD Semiquinone in Electron Transfer Flavoprotein
    • Swanson MA, Kathirvelu V, Majtan T, Frerman FE, Eaton GR, Eaton SS (2009) DEER Distance Measurement Between a Spin Label and a Native FAD Semiquinone in Electron Transfer Flavoprotein. J Am Chem Soc 131:15978-15979.
    • (2009) J Am Chem Soc , vol.131 , pp. 15978-15979
    • Swanson, M.A.1    Kathirvelu, V.2    Majtan, T.3    Frerman, F.E.4    Eaton, G.R.5    Eaton, S.S.6
  • 18
    • 0019321483 scopus 로고
    • Circular dichroism studies of acyl-CoA dehydrogenase and electron transfer flavoprotein
    • Auer HE, Frerman FE (1980) Circular dichroism studies of acyl-CoA dehydrogenase and electron transfer flavoprotein. J Biol Chem 255:8157-8163.
    • (1980) J Biol Chem , vol.255 , pp. 8157-8163
    • Auer, H.E.1    Frerman, F.E.2
  • 19
    • 0030586056 scopus 로고    scopus 로고
    • Watching proteins move using site-directed spin labeling
    • DOI 10.1016/S0969-2126(96)00085-8
    • Hubbell WL, Mchaourab HS, Altenbach C, Lietzow MA (1996) Watching proteins move using site-directed spin labeling. Structure 4:779-783. (Pubitemid 26312362)
    • (1996) Structure , vol.4 , Issue.7 , pp. 779-783
    • Hubbell, W.L.1    Mchaourab, H.S.2    Altenbach, C.3    Lietzow, M.A.4
  • 20
    • 0035951097 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: Mapping light-dependent changes in distance between residue 65 in helix TM1 and residues in the sequence 306-319 at the cytoplasmic end of helix TM7 and in helix H8
    • DOI 10.1021/bi011546g
    • Altenbach C, Cai K, Klein-Seetharaman J, Khorana HG, Hubbell WL (2001) Structure and function of rhodopsin: mapping light-dependent changes in distance between residue 65 in helix TM1 and residues in the sequence 306-319 at the cytoplasmic end of helix TM7 and in helix H8. Biochemistry 40:15483-15492. (Pubitemid 34015175)
    • (2001) Biochemistry , vol.40 , Issue.51 , pp. 15483-15492
    • Altenbach, C.1    Cai, K.2    Klein-Seetharaman, J.3    Khorana, H.G.4    Hubbell, W.L.5
  • 21
    • 0035799354 scopus 로고    scopus 로고
    • Molecular motion of spin labeled side chains in α-helices: Analysis by variation of side chain structure
    • DOI 10.1021/bi002645h
    • Columbus L, Kalai T, Jekoe J, Hideg K, Hubbell WL (2001) Molecular Motion of Spin Labeled Side Chains in α-Helices: Analysis by Variation of Side Chain Structure. Biochemistry 40:3828-3846. (Pubitemid 32280420)
    • (2001) Biochemistry , vol.40 , Issue.13 , pp. 3828-3846
    • Columbus, L.1    Kalai, T.2    Jeko, J.3    Hideg, K.4    Hubbell, W.L.5
  • 22
    • 0022373152 scopus 로고
    • Interflavin oxidation-reduction reactions between pig kidney general acyl-CoA dehydrogenase and electron-transferring flavoprotein
    • DOI 10.1021/bi00345a015
    • Gorelick RL, Schopfer LM, Ballou DP, Massey V, Thorpe C (1985) Interflavin oxidation-reduction reactions between pig kidney general acyl-CoA dehydrogenase and electron transferring-flavoprotein. Biochemistry 24:6830-6839. (Pubitemid 16170211)
    • (1985) Biochemistry , vol.24 , Issue.24 , pp. 6830-6839
    • Gorelick, R.J.1    Schopfer, L.M.2    Ballou, D.P.3
  • 23
    • 0000330099 scopus 로고
    • Application of the double resonance method to electron spin echo in a study of the spatial distribution of paramagnetic centers in solids
    • Milov AD, Salikhov KM, Shchirov MD (1981) Application of the double resonance method to electron spin echo in a study of the spatial distribution of paramagnetic centers in solids. Sov Phys Solid State 23:565-569.
    • (1981) Sov Phys Solid State , vol.23 , pp. 565-569
    • Milov, A.D.1    Salikhov, K.M.2    Shchirov, M.D.3
  • 25
    • 77954628406 scopus 로고    scopus 로고
    • Nature of the energy landscape for gated electron transfer in a dynamic redox protein
    • Hay S, Brenner S, Khara B, Quinn AM, Rigby SEJ, Scrutton NS (2010) Nature of the energy landscape for gated electron transfer in a dynamic redox protein. J Am Chem Soc 132:9738-9745.
    • (2010) J Am Chem Soc , vol.132 , pp. 9738-9745
    • Hay, S.1    Brenner, S.2    Khara, B.3    Quinn, A.M.4    Rigby, S.E.J.5    Scrutton, N.S.6
  • 26
    • 67649607260 scopus 로고    scopus 로고
    • Significantly Improved Sensitivity of Q-Band PELDOR/DEER Experiments Relative to X-Band Is Observed in Measuring the Intercoil Distance of a Leucine Zipper Motif Peptide (GCN4-LZ)
    • Ghimire H, McCarrick RM, Budil DE, Lorigan GA (2009) Significantly Improved Sensitivity of Q-Band PELDOR/DEER Experiments Relative to X-Band Is Observed in Measuring the Intercoil Distance of a Leucine Zipper Motif Peptide (GCN4-LZ). Biochemistry 48:5782-5784.
    • (2009) Biochemistry , vol.48 , pp. 5782-5784
    • Ghimire, H.1    McCarrick, R.M.2    Budil, D.E.3    Lorigan, G.A.4
  • 27
    • 77949608570 scopus 로고    scopus 로고
    • Increased sensitivity and extended range of distance measurements in spin-labeled membrane proteins: Q-band double electron-electron resonance and nanoscale bilayers
    • Zou P, Mchaourab HS (2010) Increased sensitivity and extended range of distance measurements in spin-labeled membrane proteins: Q-band double electron-electron resonance and nanoscale bilayers. Biophysical J 98:L18-L20.
    • (2010) Biophysical J , vol.98
    • Zou, P.1    Mchaourab, H.S.2
  • 29
    • 0001579637 scopus 로고
    • Double electron-electron resonance spin-echo modulation: Spectroscopic measurement of electron spin pair separations in orientationally disordered solids
    • Larsen RG, Singel DJ (1993) Double electron-electron resonance spin-echo modulation: Spectroscopic measurement of electron spin pair separations in orientationally disordered solids. J Chem Phys 98:5134-5146.
    • (1993) J Chem Phys , vol.98 , pp. 5134-5146
    • Larsen, R.G.1    Singel, D.J.2
  • 30
    • 0022073488 scopus 로고
    • Electron-spin-resonance studies on flavoenzymes
    • Edmondson DE (1985) Electron-spin-resonance studies on flavoenzymes. Biochem Soc Trans 13:593-600.
    • (1985) Biochem Soc Trans , vol.13 , pp. 593-600
    • Edmondson, D.E.1
  • 33
    • 0027218957 scopus 로고
    • Cloning, sequencing, and expression of the genes encoding subunits of Paracoccus denitrificans electron transfer flavoprotein
    • Bedzyk LA, Escudero KW, Gill RE, Griffin KJ, Frerman FE (1993) Cloning, sequencing and expression of the genes encoding the subunits of Paracoccus denitrificans electron transfer flavoprotein. J Biol Chem 268:20211-20217. (Pubitemid 23278924)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.27 , pp. 20211-20217
    • Bedzyk, L.A.1    Escudero, K.W.2    Gill, R.E.3    Griffin, K.J.4    Frerman, F.E.5
  • 34
    • 0021811007 scopus 로고
    • Partial purification and characterization of glutaryl-coenzyme A dehydrogenase, electron transfer flavoprotein, and electron transfer flavoprotein-Q oxidoreductase from Paracoccus denitrificans
    • Husain M, Steenkamp DJ (1985) Partial purification and characterization of glutaryl-coenzyme A dehydrogenase, electron transfer flavoprotein, and electron transfer flavoprotein-Q oxidoreductase from Paracoccus denitrificans. J Bacteriol 163:709-715. (Pubitemid 15008799)
    • (1985) Journal of Bacteriology , vol.163 , Issue.2 , pp. 709-715
    • Husain, M.1    Steenkamp, D.J.2
  • 35
    • 35648987515 scopus 로고    scopus 로고
    • Practical Pulsed Dipolar ESR (DEER)
    • Fajer PG, Brown L, Song L (2007) Practical Pulsed Dipolar ESR (DEER). Biol Magn Reson 27:95-128.
    • (2007) Biol Magn Reson , vol.27 , pp. 95-128
    • Fajer, P.G.1    Brown, L.2    Song, L.3
  • 36
    • 11344285129 scopus 로고    scopus 로고
    • The determination of pair distance distributions by pulsed ESR using Tikhonov regularization
    • DOI 10.1016/j.jmr.2004.10.012, PII S1090780704003532
    • Chiang Y-W, Borbat PP, Freed JH (2005) The determination of pair distance distributions by pulsed ESR using Tikhonov regularization. J Magn Reson 172:279-295. (Pubitemid 40072533)
    • (2005) Journal of Magnetic Resonance , vol.172 , Issue.2 , pp. 279-295
    • Chiang, Y.-W.1    Borbat, P.P.2    Freed, J.H.3
  • 37
    • 84986505827 scopus 로고
    • Validation of the general purpose QUANTA 3.2/CHARMm force field
    • Momany FA, Rone R (1992) Validation of the general purpose QUANTA 3.2/CHARMm force field. J Comput Chem 13:888-900.
    • (1992) J Comput Chem , vol.13 , pp. 888-900
    • Momany, F.A.1    Rone, R.2
  • 38
    • 84946636483 scopus 로고
    • Special geometrical constraints in the molecular dynamics of chain molecules
    • Ryckaert JP (1985) Special geometrical constraints in the molecular dynamics of chain molecules. Mol Phys 55:549-556.
    • (1985) Mol Phys , vol.55 , pp. 549-556
    • Ryckaert, J.P.1
  • 39
    • 0035857235 scopus 로고    scopus 로고
    • Influence of solvent polarity and hydrogen bonding on the EPR parameters of a nitroxide spin label studied by 9-GHz and 95-GHz EPR spectroscopy and DFT calculations
    • DOI 10.1021/jp0116914
    • Owenius R, Engstroem M, Lindgren M, Huber M (2001) Influence of Solvent Polarity and Hydrogen Bonding on the EPR Parameters of a Nitroxide Spin Label Studied by 9-GHz and 95-GHz EPR Spectroscopy and DFT Calculations. J Phys Chem A 105:10967-10977. (Pubitemid 35378583)
    • (2001) Journal of Physical Chemistry A , vol.105 , Issue.49 , pp. 10967-10977
    • Owenius, R.1    Engstrom, M.2    Lindgren, M.3    Huber, M.4
  • 40
    • 0039102400 scopus 로고
    • ESR and ENDOR studies on sarcosine dehydrogenase, acyl-CoA dehydrogenase and electron transfer flavoproteins
    • Massey V, Williams CH, Jr., Ed. New York: Elsevier
    • McKean MC, Sealy RC, Frerman FE, ESR and ENDOR studies on sarcosine dehydrogenase, acyl-CoA dehydrogenase and electron transfer flavoproteins. In: Massey V, Williams CH, Jr., Ed. (1982) Flavins and Flavoproteins. New York: Elsevier, pp 614-617.
    • (1982) Flavins and Flavoproteins , pp. 614-617
    • McKean, M.C.1    Sealy, R.C.2    Frerman, F.E.3
  • 41
    • 33947291976 scopus 로고
    • Electron spin resonance study of the copper(II) chelates of certain monothio-b-diketones and diethyldithiocarbamate
    • Toy AD, Chaston SHH, Pilbrow JR, Smith TD (1971) Electron spin resonance study of the copper(II) chelates of certain monothio-b-diketones and diethyldithiocarbamate. Inorg Chem 10:2219-2225.
    • (1971) Inorg Chem , vol.10 , pp. 2219-2225
    • Toy, A.D.1    Chaston, S.H.H.2    Pilbrow, J.R.3    Smith, T.D.4


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