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Volumn 107, Issue 5, 2010, Pages 1930-1935

Direct assignment of EPR spectra to structurally defined iron-sulfur clusters in complex I by double electron-electron resonance

Author keywords

DEER; Distance measurement; Mitochondria; NADH:quinone oxidoreductase; Pulsed EPR

Indexed keywords

IRON SULFUR PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE);

EID: 76649102458     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0908050107     Document Type: Article
Times cited : (110)

References (29)
  • 1
    • 0037972522 scopus 로고    scopus 로고
    • Mitochondrial respiratory-chain diseases
    • DiMauro S, Schon EA (2003) Mitochondrial respiratory-chain diseases. New Engl J Med, 348:2656-2668.
    • (2003) New Engl J Med , vol.348 , pp. 2656-2668
    • DiMauro, S.1    Schon, E.A.2
  • 2
    • 33644872938 scopus 로고    scopus 로고
    • Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus
    • Sazanov LA, Hinchliffe P (2006) Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus. Science, 311:1430-1436.
    • (2006) Science , vol.311 , pp. 1430-1436
    • Sazanov, L.A.1    Hinchliffe, P.2
  • 3
    • 0032490089 scopus 로고    scopus 로고
    • Iron-sulfur clusters/semiquinones in complex I
    • Ohnishi T (1998) Iron-sulfur clusters/semiquinones in complex I. Biochim Biophys Acta, 1364:186-206.
    • (1998) Biochim Biophys Acta , vol.1364 , pp. 186-206
    • Ohnishi, T.1
  • 4
    • 50949130428 scopus 로고    scopus 로고
    • Were there any " misassignments" among iron-sulfur clusters N4, N5 and N6b in NADH-quinone oxidoreductase (complex I)?
    • Ohnishi T, Nakamaru-Ogiso E (2008) Were there any " misassignments" among iron-sulfur clusters N4, N5 and N6b in NADH-quinone oxidoreductase (complex I)?. Biochim Biophys Acta, 1777:703-710.
    • (2008) Biochim Biophys Acta , vol.1777 , pp. 703-710
    • Ohnishi, T.1    Nakamaru-Ogiso, E.2
  • 5
    • 34547917597 scopus 로고    scopus 로고
    • Reevaluating the relationship between EPR spectra and enzyme structure for the iron-sulfur clusters in NADH-quinone oxidoreductase
    • Yakovlev G, Reda T, Hirst J (2007) Reevaluating the relationship between EPR spectra and enzyme structure for the iron-sulfur clusters in NADH-quinone oxidoreductase. Proc Natl Acad Sci USA, 104:12720-12725.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 12720-12725
    • Yakovlev, G.1    Reda, T.2    Hirst, J.3
  • 8
    • 0033523919 scopus 로고    scopus 로고
    • Natural engineering principles of electron tunnelling in biological oxidation-reduction
    • Page CC, Moser CC, Chen X, Dutton PL (1999) Natural engineering principles 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
  • 9
    • 0027990677 scopus 로고
    • Thermodynamic analysis of flavin in mitochondrial NADH:ubiquinone oxidoreductase (complex I)
    • Sled VD, Rudnitzky NI, Hatefi Y, Ohnishi T (1994) Thermodynamic analysis of flavin in mitochondrial NADH:ubiquinone oxidoreductase (complex I). Biochemistry, 33:10069-10075.
    • (1994) Biochemistry , vol.33 , pp. 10069-10075
    • Sled, V.D.1    Rudnitzky, N.I.2    Hatefi, Y.3    Ohnishi, T.4
  • 10
    • 13444259531 scopus 로고    scopus 로고
    • NF) and the interaction with cluster N2: New insight into the energy-coupled electron transfer in complex I
    • NF) and the interaction with cluster N2: New insight into the energy-coupled electron transfer in complex I. Biochemistry, 44:1744-1754.
    • (2005) Biochemistry , vol.44 , pp. 1744-1754
    • Yano, T.1    Dunham, W.R.2    Ohnishi, T.3
  • 11
    • 0037112592 scopus 로고    scopus 로고
    • Distance measurements in the nanometer range by pulse EPR
    • Jeschke G (2002) Distance measurements in the nanometer range by pulse EPR. Chemphyschem, 3:927-932.
    • (2002) Chemphyschem , vol.3 , pp. 927-932
    • Jeschke, G.1
  • 12
    • 0036290220 scopus 로고    scopus 로고
    • Direct conversion of EPR dipolar time evolution data to distance distributions
    • Jeschke G, Koch A, Jonas U, Godt A (2002) Direct conversion of EPR dipolar time evolution data to distance distributions. J Magn Reson, 155:72-82.
    • (2002) J Magn Reson , vol.155 , pp. 72-82
    • Jeschke, G.1    Koch, A.2    Jonas, U.3    Godt, A.4
  • 13
    • 28044472953 scopus 로고    scopus 로고
    • Maximum entropy: A complement to Tikhonov regularization for determination of pair distance distributions by pulsed ESR
    • Chiang Y-W, Borbat PP, Freed JH (2005) Maximum entropy: A complement to Tikhonov regularization for determination of pair distance distributions by pulsed ESR. J Magn Reson, 177:184-196.
    • (2005) J Magn Reson , vol.177 , pp. 184-196
    • Chiang, Y.-W.1    Borbat, P.P.2    Freed, J.H.3
  • 14
    • 0028283695 scopus 로고
    • Biological polynuclear clusters coupled by magnetic interactions-from the point dipole approximation to a local spin model
    • Bertrand P, et al. (1994) Biological polynuclear clusters coupled by magnetic interactions-from the point dipole approximation to a local spin model. J Am Chem Soc, 116:3078-3086.
    • (1994) J Am Chem Soc , vol.116 , pp. 3078-3086
    • Bertrand, P.1
  • 15
    • 0029467008 scopus 로고
    • Orbital interactions, electron delocalization and spin coupling in iron-sulfur clusters
    • Noodleman L, Peng CY, Case DA, Mouesca JM (1995) Orbital interactions, electron delocalization and spin coupling in iron-sulfur clusters. Coord Chem Rev, 144:199-244.
    • (1995) Coord Chem Rev , vol.144 , pp. 199-244
    • Noodleman, L.1    Peng, C.Y.2    Case, D.A.3    Mouesca, J.M.4
  • 16
    • 0037164101 scopus 로고    scopus 로고
    • Pulsed electron-electron double resonance on multinuclear metal clusters: Assignment of spin projection factors based on the dipolar interaction
    • Elsässer C, Brecht M, Bittl R (2002) Pulsed electron-electron double resonance on multinuclear metal clusters: Assignment of spin projection factors based on the dipolar interaction. J Am Chem Soc, 124:12606-12611.
    • (2002) J Am Chem Soc , vol.124 , pp. 12606-12611
    • Elsässer, C.1    Brecht, M.2    Bittl, R.3
  • 17
    • 14644437752 scopus 로고    scopus 로고
    • Treatment of spin-coupled metal-centers in pulsed electron-electron double-resonance experiments
    • Elsaesser C, Brecht M, Bittl R (2005) Treatment of spin-coupled metal-centers in pulsed electron-electron double-resonance experiments. Biochem Soc Trans, 33:15-19.
    • (2005) Biochem Soc Trans , vol.33 , pp. 15-19
    • Elsaesser, C.1    Brecht, M.2    Bittl, R.3
  • 18
    • 28844486080 scopus 로고    scopus 로고
    • EasySpin, a comprehensive software package for spectral simulation and analysis in EPR
    • Stoll S, Schweiger A (2006) EasySpin, a comprehensive software package for spectral simulation and analysis in EPR. J Magn Reson, 178:42-55.
    • (2006) J Magn Reson , vol.178 , pp. 42-55
    • Stoll, S.1    Schweiger, A.2
  • 19
    • 68349114810 scopus 로고    scopus 로고
    • Structural information from orientationally selective DEER spectroscopy
    • Lovett JE, et al. (2009) Structural information from orientationally selective DEER spectroscopy. Phys Chem Chem Phys, 11:6840-6848.
    • (2009) Phys Chem Chem Phys , vol.11 , pp. 6840-6848
    • Lovett, J.E.1
  • 20
    • 33645655818 scopus 로고    scopus 로고
    • Identification of a novel subunit of respiratory complex I from Thermus thermophilus
    • Hinchliffe P, Carroll J, Sazanov LA (2006) Identification of a novel subunit of respiratory complex I from Thermus thermophilus. Biochemistry, 45:4413-4420.
    • (2006) Biochemistry , vol.45 , pp. 4413-4420
    • Hinchliffe, P.1    Carroll, J.2    Sazanov, L.A.3
  • 21
    • 0029075136 scopus 로고
    • Isolation and characterization of the proton-translocating NADH:ubiquinone oxidoreductase from Escherichia coli
    • Leif H, Sled VD, Ohnishi T, Weiss H, Friedrich T (1995) Isolation and characterization of the proton-translocating NADH:ubiquinone oxidoreductase from Escherichia coli. Eur J Biochem, 230:538-548.
    • (1995) Eur J Biochem , vol.230 , pp. 538-548
    • Leif, H.1    Sled, V.D.2    Ohnishi, T.3    Weiss, H.4    Friedrich, T.5
  • 23
    • 0030868605 scopus 로고    scopus 로고
    • Iron-sulfur clusters: Nature's modular, multipurpose structures
    • Beinert H, Holm RH, Münck E (1997) Iron-sulfur clusters: Nature's modular, multipurpose structures. Science, 277:653-659.
    • (1997) Science , vol.277 , pp. 653-659
    • Beinert, H.1    Holm, R.H.2    Münck, E.3
  • 24
    • 0034454768 scopus 로고    scopus 로고
    • Mössbauer studies of exchange coupled cluster assemblies in biological systems
    • Münck E, Popescu CV (2000) Mössbauer studies of exchange coupled cluster assemblies in biological systems. Hyperfine Interact, 126:59-67.
    • (2000) Hyperfine Interact , vol.126 , pp. 59-67
    • Münck, E.1    Popescu, C.V.2
  • 25
    • 0030980887 scopus 로고    scopus 로고
    • Low temperature EPR on Photosystem I single crystals: Orientation of the iron-sulfur centers FA and FB
    • Kamlowski A, van der Est A, Fromme P, Stehlik D (1997) Low temperature EPR on Photosystem I single crystals: Orientation of the iron-sulfur centers FA and FB. Biochim Biophys Acta, 1319:185-198.
    • (1997) Biochim Biophys Acta , vol.1319 , pp. 185-198
    • Kamlowski, A.1    van der Est, A.2    Fromme, P.3    Stehlik, D.4
  • 27
    • 0000384069 scopus 로고
    • Spin-densities and spin coupling in iron-sulfur clusters-a new analysis of hyperfine coupling-constants
    • Mouesca JM, Noodleman L, Case DA, Lamotte B (1995) Spin-densities and spin coupling in iron-sulfur clusters-a new analysis of hyperfine coupling-constants. Inorg Chem, 34:4347-4359.
    • (1995) Inorg Chem , vol.34 , pp. 4347-4359
    • Mouesca, J.M.1    Noodleman, L.2    Case, D.A.3    Lamotte, B.4
  • 28
    • 14044262235 scopus 로고    scopus 로고
    • 4] cluster N5 but is required for catalytic activity
    • 4] cluster N5 but is required for catalytic activity. J Biol Chem, 280:5622-5625.
    • (2005) J Biol Chem , vol.280 , pp. 5622-5625
    • Waletko, A.1
  • 29
    • 30144445462 scopus 로고    scopus 로고
    • Phospholipid interactions determine the catalytic activity of NADH:ubiquinone oxidoreductase (complex I) from bovine mitochondria
    • Sharpley MS, Shannon RJ, Draghi F, Hirst J (2006) Phospholipid interactions determine the catalytic activity of NADH:ubiquinone oxidoreductase (complex I) from bovine mitochondria. Biochemistry, 45:241-248.
    • (2006) Biochemistry , vol.45 , pp. 241-248
    • Sharpley, M.S.1    Shannon, R.J.2    Draghi, F.3    Hirst, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.