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Volumn 43, Issue 2, 2010, Pages 181-189

Multifrequency pulsed electron paramagnetic resonance on metalloproteins

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; COPPER; CYTOCHROME C; CYTOCHROME C OXIDASE; FUNGAL PROTEIN; IRON; METALLOPROTEIN;

EID: 77249165548     PISSN: 00014842     EISSN: 15204898     Source Type: Journal    
DOI: 10.1021/ar900050d     Document Type: Article
Times cited : (20)

References (68)
  • 2
    • 0038506974 scopus 로고    scopus 로고
    • ENDOR of metalloenzymes
    • Hoffman, B. M. ENDOR of Metalloenzymes. Ace. Chem. Res. 2003, 36, 522-529.
    • (2003) Ace. Chem. Res. , vol.36 , pp. 522-529
    • Hoffman, B.M.1
  • 3
    • 0000261066 scopus 로고
    • ENDOR of randomly oriented mononuclear metalloproteins toward structural determinations of the prosthetic group
    • Berliner, L. J., Reuben, J., Eds.; Kluwer Academic Publishers: New York, Chapter 5
    • Huettermann, J. ENDOR of Randomly Oriented Mononuclear Metalloproteins Toward Structural Determinations of the Prosthetic Group. In Biological Magnetic Resonanse, Berliner, L. J., Reuben, J., Eds.; Kluwer Academic Publishers: New York, 1993; Vol.13, Chapter 5.
    • (1993) Biological Magnetic Resonanse , vol.13
    • Huettermann, J.1
  • 4
    • 0034743154 scopus 로고    scopus 로고
    • Pulsed EPR spectroscopy: Biological applications
    • DOI 10.1146/annurev.physchem.52.1.279
    • Prisner, T. F.; Rohrer, M.; MacMlllan, F. Pulsed EPR Spectroscopy: Biological Applications. Annu. Rev. Phys. Chem. 2001, 52, 279-313. (Pubitemid 33655125)
    • (2001) Annual Review of Physical Chemistry , vol.52 , pp. 279-313
    • Prisner, T.1    Rohrer, M.2    MacMillan, F.3
  • 5
    • 0001773735 scopus 로고    scopus 로고
    • Distance measurements in biological systems by EPR
    • Berliner L. J., Eaten, S. S., Eaten, G. R., Eds. Kluwer Academic Publishers: New York
    • Berliner L. J., Eaten, S. S., Eaten, G. R., Eds. Distance Measurements in Biological Systems by EPR. Biological Magnetic Resonanse, Kluwer Academic Publishers: New York, 2000; Vol.19.
    • (2000) Biological Magnetic Resonanse , vol.19
  • 6
    • 0037164101 scopus 로고    scopus 로고
    • Pulsed electron-electron double resonance on multinuclear metal clusters: Assignment of spin projection factors based on the dipolar interaction
    • DOI 10.1021/ja027348
    • Elsaesser, C; Brecht, M.; Bittl, R. Pulsed Electron-Electron Double Resonance on Multinuclear Metal Clusters: Assignment of Spin Projection Factors Based on the Dipolar Interaction. J. Am. Chem. Soc. 2002, 124, 12606-12611. (Pubitemid 35204587)
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.42 , pp. 12606-12611
    • Elsasser, C.1    Brecht, M.2    Bittl, R.3
  • 8
    • 34548567870 scopus 로고    scopus 로고
    • Measuring distances in proteins by saturation-recovery EPR
    • Hirsh, J. D.; Brudvig, G. W. Measuring Distances in Proteins by Saturation-Recovery EPR. Nat. Protoc. 2007, 27, 1770-1781.
    • (2007) Nat. Protoc. , vol.27 , pp. 1770-1781
    • Hirsh, J.D.1    Brudvig, G.W.2
  • 9
    • 34548317408 scopus 로고    scopus 로고
    • Long-range distance determinations in blomacromelecules by EPR spectroscopy
    • Schiemann, O.; Prisner, T. F. Long-Range Distance Determinations in Blomacromelecules by EPR Spectroscopy. Q. Rev. Biophys. 2007, 40, 1-53.
    • (2007) Q. Rev. Biophys. , vol.40 , pp. 1-53
    • Schiemann, O.1    Prisner, T.F.2
  • 10
    • 0002881384 scopus 로고
    • ESEEM and LEFE of metalloproteins and model compounds
    • Hoff, A. J., Ed.; Elsevier: Amsterdam, Chapter 1
    • Mims W. B., Peisach J., ESEEM and LEFE of Metalloproteins and Model Compounds. In Advanced EPR: Application to biology and biochemistry, Hoff, A. J., Ed.; Elsevier: Amsterdam, 1989; Chapter 1.
    • (1989) Advanced EPR: Application to Biology and Biochemistry
    • Mims, W.B.1    Peisach, J.2
  • 11
    • 35048826863 scopus 로고    scopus 로고
    • [NiFe] and [FeFe] hydrogenases studied by advanced magnetic resonance techniques
    • van Gastei, M.; Reijerse, E. J.; Lubitz, W. [NiFe] and [FeFe] Hydrogenases Studied by Advanced Magnetic Resonance Techniques. Chem. Rev. 2007, 107, 4331-4365.
    • (2007) Chem. Rev. , vol.107 , pp. 4331-4365
    • Van Gastei, M.1    Reijerse, E.J.2    Lubitz, W.3
  • 12
    • 34547992643 scopus 로고    scopus 로고
    • The strength of EPR and ENDOR techniques in revealing structure-function relationships in metalloproteins
    • Van Doorslaer, S.; Vinck, E. The Strength of EPR and ENDOR Techniques in Revealing Structure-Function Relationships in Metalloproteins. Phys. Chem. Chem. Phys. 2007, 9, 4620-11638
    • (2007) Phys. Chem. Chem. Phys. , vol.9 , pp. 4620-11638
    • Van Doorslaer, S.1    Vinck, E.2
  • 13
    • 0034350315 scopus 로고    scopus 로고
    • Electron spin echo envelope modulation (ESEEM) spectroscopy as a tool to investigate the coordination environment of metal centers
    • Doligiannakis, Y.; Louloudi, M.; Hadjiliadls, N. Electron Spin Echo Envelope Modulation (ESEEM) Spectroscopy As a Tool to Investigate the Coordination Environment of Metal Centers. Coord. Chem. Rev. 2000, 204, 1-112.
    • (2000) Coord. Chem. Rev. , vol.204 , pp. 1-112
    • Doligiannakis, Y.1    Louloudi, M.2    Hadjiliadls, N.3
  • 16
    • 30144433447 scopus 로고    scopus 로고
    • High-frequency 95 GHz ENDOR characterizes the metal binding sites in wild-type p21 Ras GDP and its oncogenic mutant G12V in frozen solution
    • Bcnnati, M.; Hertel, M. M.; Prisner, T. F.; Weiden, N.; Hofweber, R.; Spoemer, M.; Horn, G.; Kalbitzer, H.-R. High-Frequency 95 GHz ENDOR Characterizes the Metal Binding Sites in Wild-Type p21 Ras GDP and its Oncogenic Mutant G12V in Frozen Solution. Biochemistry 2006, 45, 42-50.
    • (2006) Biochemistry , vol.45 , pp. 42-50
    • Bcnnati, M.1    Hertel, M.M.2    Prisner, T.F.3    Weiden, N.4    Hofweber, R.5    Spoemer, M.6    Horn, G.7    Kalbitzer, H.-R.8
  • 19
    • 59149103868 scopus 로고    scopus 로고
    • Structures and reaction pathways of the molybdenum centres of suite-oxidizing enzymes by pulsed EPR spectroscopy
    • Enemark, J. H.; Astashkin, A. V.; Raitsimring, A. M. Structures and Reaction Pathways of the Molybdenum Centres of Suite-Oxidizing Enzymes by Pulsed EPR Spectroscopy. Biochem. Soc. Trans. 2008, 36, 1129-1133.
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 1129-1133
    • Enemark, J.H.1    Astashkin, A.V.2    Raitsimring, A.M.3
  • 20
    • 77249109188 scopus 로고    scopus 로고
    • New Methods in electron paramagnetic resonance spectroscopy for structure and function determination in biological systems
    • Quinkert, G., Ed.; Helvetica Chimica Acta; Wiley: Weinheim, Germany, Chapter 3
    • Prisner, T F. New Methods in Electron Paramagnetic Resonance Spectroscopy for Structure and Function Determination In Biological Systems. In Essays in Contemporary Chemistry: From Molecular Structure towards Biology, Quinkert, G., Ed.; Helvetica Chimica Acta; Wiley: Weinheim, Germany, 2001 ; Chapter 3, pp 1 -23.
    • (2001) Essays in Contemporary Chemistry: from Molecular Structure Towards Biology , pp. 1-23
    • Prisner, T.F.1
  • 22
    • 0035976005 scopus 로고    scopus 로고
    • Electron spin echo envelope modulation spectroscopy in photosystem I
    • Doligiannakis, Yiannis; Rutherford, A. W. Electron Spin Echo Envelope Modulation Spectroscopy in Photosystem I. Biochlm. Biophys. Acta 2001, 1507, 226-246.
    • (2001) Biochlm. Biophys. Acta , vol.1507 , pp. 226-246
    • Doligiannakis, Y.1    Rutherford, A.W.2
  • 23
    • 0000242143 scopus 로고
    • Hyperfine sublevei correlation (hyscore) spectroscopy: A 2D ESR investigation of the squaric acid radical
    • Höfer, P.; Grupp, A.; Nebenführ, H.; Mehring, M. Hyperfine Sublevei Correlation (Hyscore) Spectroscopy: A 2D ESR Investigation of the Squaric Acid Radical. Chem. Phys. Lett 1986, 132, 279-282.
    • (1986) Chem. Phys. Lett , vol.132 , pp. 279-282
    • Höfer, P.1    Grupp, A.2    Nebenführ, H.3    Mehring, M.4
  • 24
    • 0000830570 scopus 로고
    • Multifrequency ESEEM: Perspectives and applications
    • Hoff, A. J., Ed.; Elsevier: Amsterdam, Chapter 3
    • Singol, D. J. Multifrequency ESEEM: Perspectives and Applications. In Advanced EPR: Application to Biology and Biochemistry, Hoff, A. J., Ed.; Elsevier: Amsterdam, 1989; Chapter 3.
    • (1989) Advanced EPR: Application to Biology and Biochemistry
    • Singol, D.J.1
  • 25
    • 3042596865 scopus 로고    scopus 로고
    • Spin distribution and the location of protons in paramagnetic proteins
    • Goldfarb, D.; Arieli, D. Spin Distribution and the Location of Protons in Paramagnetic Proteins. Annu. Rev. Biophys. Biomol. Struct. 2004, 33, 441-1168
    • (2004) Annu. Rev. Biophys. Biomol. Struct. , vol.33 , pp. 441-1168
    • Goldfarb, D.1    Arieli, D.2
  • 26
    • 0001209778 scopus 로고    scopus 로고
    • Pulsed high-frequency/high-field EPR
    • Prisner, T. F. Pulsed High-Frequency/High-Field EPR. Adv. Magn. Opt Reson. 1997, 20, 245-299.
    • (1997) Adv. Magn. Opt Reson. , vol.20 , pp. 245-299
    • Prisner, T.F.1
  • 27
    • 0002279727 scopus 로고
    • Electron-electron double resonance in electron spin echo: Model biradlcal systems and the sensitized photolysis of decalin
    • Milov, A. D.; Ponomarev, A. B.; Tsvetkov, Yu. D. Electron-Electron Double Resonance in Electron Spin Echo: Model Biradlcal Systems and the Sensitized Photolysis of Decalin. Chem. Phys. Lett. 1984, 110, 67-72.
    • (1984) Chem. Phys. Lett. , vol.110 , pp. 67-72
    • Milov, A.D.1    Ponomarev, A.B.2    Tsvetkov, Y.D.3
  • 28
    • 0001579637 scopus 로고
    • Double electron-electron resonance spin-echo modulation: Spectroscopic measurement of electron spin pair separations in orientationally disordered solids
    • Larsen, R. G.; Singel, D. J. Double Electron-Electron Resonance Spin-Echo Modulation: Spectroscopic Measurement of Electron Spin Pair Separations in Orientationally Disordered Solids. J. Chem. Phys. 1993, 98, 5134-5146.
    • (1993) J. Chem. Phys. , vol.98 , pp. 5134-5146
    • Larsen, R.G.1    Singel, D.J.2
  • 29
    • 0036934905 scopus 로고    scopus 로고
    • Measurement of diffusion coefficients of additive molecules in colloidal polymer particles by electron paramagnetic resonance
    • DOI 10.1007/s00396-001-0637-0
    • Jeschke, G. Determination of the Nanostructure of Polymer Materials by Electron Paramagnetic Resonance Spectroscopy. Macromol. Rapid Commun. 2002, 23, 227-246. (Pubitemid 36075847)
    • (2002) Colloid and Polymer Science , vol.280 , Issue.6 , pp. 569-573
    • Cramer, S.E.1    Jeschke, G.2    Spiess, H.W.3
  • 30
    • 0033660661 scopus 로고    scopus 로고
    • New technologies in electron spin resonance
    • Freed, J. H. New Technologies In Electron Spin Resonance. Annu. Rev. Phys. Chem. 2000, 51, 655-689.
    • (2000) Annu. Rev. Phys. Chem. , vol.51 , pp. 655-689
    • Freed, J.H.1
  • 31
    • 0000890494 scopus 로고
    • The theory of electron spin-echo signal decay resulting from dipole-dipole interactions between paramagnetic centers in solids
    • Sallkhov, K. M.; Dzuba, S. A.; Raitsimring, A. M. The Theory of Electron Spin-Echo Signal Decay Resulting from Dipole-Dipole Interactions between Paramagnetic Centers in Solids. J. Magn. Reson. 1981, 42, 255-276.
    • (1981) J. Magn. Reson. , vol.42 , pp. 255-276
    • Sallkhov, K.M.1    Dzuba, S.A.2    Raitsimring, A.M.3
  • 32
    • 41149139468 scopus 로고    scopus 로고
    • Probing the homo-pocket structure of the paramagnetic fornis of cytoglobin and a distal hlstidine mutant using electron paramagnetic resonance
    • loanftescu, A. I.; Van Doorslaor, S.; Dewilde, S.; Endeward, B.; Moens, L Probing the Homo-Pocket Structure of the Paramagnetic Fornis of Cytoglobin and a Distal Hlstidine Mutant Using Electron Paramagnetic Resonance. Mol. Phys. 2007, 105, 2073-2086.
    • (2007) Mol. Phys. , vol.105 , pp. 2073-2086
    • Loanftescu, A.I.1    Van Doorslaor, S.2    Dewilde, S.3    Endeward, B.4    Moens, L.5
  • 33
    • 33748744224 scopus 로고    scopus 로고
    • Identification of hydrogen bonds to the rieske cluster through the weakly coupled nitrogens detected by electron spin echo envelope modulation spectroscopy
    • Dikanov, S. A.; Kolling, D. R. J.; Endeward, B.; Samoilova, R. I.; Prisner, T. F.; Nair, S. K.; Crofts, A R. Identification of Hydrogen Bonds to the Rieske Cluster through the Weakly Coupled Nitrogens Detected by Electron Spin Echo Envelope Modulation Spectroscopy. J. Biol. Chem. 2006, 281, 27416-27425.
    • (2006) J. Biol. Chem. , vol.281 , pp. 27416-27425
    • Dikanov, S.A.1    Kolling, D.R.J.2    Endeward, B.3    Samoilova, R.I.4    Prisner, T.F.5    Nair, S.K.6    Crofts, A.R.7
  • 34
    • 0033728417 scopus 로고    scopus 로고
    • Investigation of the mn binding site in cytochrome C oxidase by high-frequency EPR
    • Käss, H.; MacMlllan, F.; Ludwig, B.; Prisner, T. F. Investigation of the Mn Binding Site in Cytochrome c Oxidase by High-Frequency EPR. J. Phys. Chem. B 2000, 104, 5362-5371.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 5362-5371
    • Käss, H.1    MacMlllan, F.2    Ludwig, B.3    Prisner, T.F.4
  • 35
    • 12444273845 scopus 로고    scopus 로고
    • Pulsed high-frequency EPR: Biological applications
    • Grinhorg, O, Berliner, L. J., Eds.; Plenum: New York Chapter 8
    • Prisner, T. F. Pulsed High-Frequency EPR: Biological Applications. In Biological Magnetic Resonance, Grinhorg, O, Berliner, L. J., Eds.; Plenum: New York 2004; Vol.22, Chapter 8.
    • (2004) Biological Magnetic Resonance , vol.22
    • Prisner, T.F.1
  • 36
    • 34547905430 scopus 로고    scopus 로고
    • Role of tyrosine-34 in the anion binding equilibria in manganese(II) superoxide dismutases
    • DOI 10.1021/bi700438j
    • Tabares, L. C; Cortez, N.; Un, S. Role of Tyrosine-34 in the Anion Binding Equilibria In Manganese(ll) Superoxide Dlsmutases. Biochemistry 2007, 46, 9320-9327. (Pubitemid 47255044)
    • (2007) Biochemistry , vol.46 , Issue.32 , pp. 9320-9327
    • Tabares, L.C.1    Cortez, N.2    Un, S.3
  • 37
    • 1542287644 scopus 로고    scopus 로고
    • Mangancso(II) zerofield interaction in camhialistic and manganese superoxide dlsmutases and its relationship to the structure of the metal binding site
    • Un, S.; Tabares, L. C.; Cortez, N.; Hiraoka, B. Y.; Yamakura, F. Mangancso(II) ZeroField Interaction in Camhialistic and Manganese Superoxide Dlsmutases and Its Relationship to the Structure of the Metal Binding Site. J. Am. Chem. Soc. 2004, 126, 2720-2726.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 2720-2726
    • Un, S.1    Tabares, L.C.2    Cortez, N.3    Hiraoka, B.Y.4    Yamakura, F.5
  • 39
    • 24344485526 scopus 로고    scopus 로고
    • New development in high field EPR with potential applications in structural biology
    • Bennati, M.; Prisner, T. F. New Development In High Field EPR with Potential Applications in Structural Biology. Rep. Prog. Phys. 2005, 68, 411-448.
    • (2005) Rep. Prog. Phys. , vol.68 , pp. 411-448
    • Bennati, M.1    Prisner, T.F.2
  • 40
    • 41249088477 scopus 로고    scopus 로고
    • Structure of the tyrosyl biradical in mouse R2 ribonucleotide reductase from high-field PELDOR
    • Denysenkov, V.; Biglino, D.; Lubitz, W.; Prisner, T F.; Bennati, M. Structure of the Tyrosyl Biradical in Mouse R2 Ribonucleotide Reductase from High-Field PELDOR. Angew. Chem., Int. Ed. 2008, 47, 1224-1227.
    • (2008) Angew. Chem., Int. Ed. , vol.47 , pp. 1224-1227
    • Denysenkov, V.1    Biglino, D.2    Lubitz, W.3    Prisner, T.F.4    Bennati, M.5
  • 41
    • 33748630529 scopus 로고    scopus 로고
    • High-held PELDOR for structure determination in protein complexes: The relative orientation of the tyrosyl in the homodimer of the e coli r2 ribonucleotide reductase
    • Denysenkov, V.; Prisner, T. F.; Stubbe, J.; Bennati, M. High-Held PELDOR for Structure Determination in Protein Complexes: The Relative Orientation of the Tyrosyl In the Homodimer of the E coli R2 Ribonucleotide Reductase. Proc. Natl. Acad. Sci. U.S.A. 2006, 103, 13386-13390.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 13386-13390
    • Denysenkov, V.1    Prisner, T.F.2    Stubbe, J.3    Bennati, M.4
  • 42
    • 1842591336 scopus 로고    scopus 로고
    • Relaxation filtered hyperfine (RERNE) spectroscopy: A tool for studying overlapping biological EPR signals
    • Maly, T.; MacMillan, F.; Zwicker, K.; Kashani-Poor, N.; Brandt, U.; Prisner, T. F. Relaxation Filtered Hyperfine (RERNE) Spectroscopy: A Tool for Studying Overlapping Biological EPR Signals. Bmchemistry 2004, 43, 3969-3978.
    • (2004) Bmchemistry , vol.43 , pp. 3969-3978
    • Maly, T.1    MacMillan, F.2    Zwicker, K.3    Kashani-Poor, N.4    Brandt, U.5    Prisner, T.F.6
  • 43
    • 4243092640 scopus 로고    scopus 로고
    • Relaxation filtered hyperfine spectroscopy (RERNE)
    • MaIy, T; Prisner. T. F. Relaxation Filtered Hyperfine Spectroscopy (RERNE). J. Magn. Reson. 2004, 170, 88-96.
    • (2004) J. Magn. Reson. , vol.170 , pp. 88-96
    • Maiy, T.1    Prisner, T.F.2
  • 44
    • 42749085624 scopus 로고    scopus 로고
    • 2D-REFINE spectroscopy: Separation of overlapping hyperfine spectra
    • Cernescu, A.; Maly, T.; Prisner, T F. 2D-REFINE Spectroscopy: Separation of Overlapping Hyperfine Spectra. J. Magn. Reson. 2008, 792, 78-84.
    • (2008) J. Magn. Reson. , vol.792 , pp. 78-84
    • Cernescu, A.1    Maly, T.2    Prisner, T.F.3
  • 45
    • 0032449962 scopus 로고    scopus 로고
    • Anaerobic respiration with elemental sulfur and with disulfides
    • DOI 10.1016/S0168-6445(98)00035-7, PII S0168644598000357
    • Hedderich, R.; Klimmek O.; Kröger, A.; Dirmeier, R.; Keller, M.; Stteter, K. O. Anaerobic Respiration with Elemental Sulfur and with Disulfides. FEMS Microbiol. Rev. 1998, 22, 353-381. (Pubitemid 29074342)
    • (1998) FEMS Microbiology Reviews , vol.22 , Issue.5 , pp. 353-381
    • Hedderich, R.1    Klimmek, O.2    Kroger, A.3    Dirmeier, R.4    Keller, M.5    Stetter, K.O.6
  • 46
    • 0004186170 scopus 로고    scopus 로고
    • Molybdenum and tungsten: Their role in biological processes
    • Sigel A., Sigel H., Eds. Marcel Dekker: New York
    • Sigel A., Sigel H., Eds. Molybdenum and Tungsten: Their Role in Biological Processes. In Metal Ions in Biological Systems, Marcel Dekker: New York, 2001 ; Vol.39.
    • (2001) Metal Ions in Biological Systems , vol.39
  • 47
    • 0038627545 scopus 로고    scopus 로고
    • Multifrequency cw-EPR investigation of the catalytic molybdenum cofactor of polysulfide reductase from Wolinella succinogenes
    • Prisner, T.; Lyubenova, S.; Atabay, Y.; MacMlllan, F.; Kroger, A.; Klimmek, O. Multifrequency cw-EPR Investigation of the Catalytic Molybdenum Cofactor of Pofysulifde Reductase from Wolinella succinogenes. J. Biol. Inorg. Chem. 2003, 8, 419-426. (Pubitemid 36578193)
    • (2003) Journal of Biological Inorganic Chemistry , vol.8 , Issue.4 , pp. 419-426
    • Prisner, T.1    Lyubenova, S.2    Atabay, Y.3    MacMillan, F.4    Kroger, A.5    Klimmek, O.6
  • 50
    • 0021769852 scopus 로고
    • Two protons are pumped from the mitochondrial matrix per electron transferred between NADH and ubiquinone
    • Wikstroem, M. Two Protons Are Pumped from the Mitochondrial Matrix Per Electron Transferred between NADH and Ubiquinone. FEBS Lett. 1984, 169, 300-304.
    • (1984) FEBS Lett. , vol.169 , pp. 300-304
    • Wikstroem, M.1
  • 51
    • 33750347347 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
    • DOI 10.1038/nature05292, PII NATURE05292
    • Lin, M. T.; Beal, M. F. Mitochondrial Dysfunction and Oxidative Stress in Neurodegenerative Diseases. Nature 2006, 443, 787-795. (Pubitemid 44622683)
    • (2006) Nature , vol.443 , Issue.7113 , pp. 787-795
    • Lin, M.T.1    Beal, M.F.2
  • 52
    • 13944278132 scopus 로고    scopus 로고
    • Mitochondria, oxidants, and aging
    • Balaban, R. S.; Nemoto, S.; Finkel, T. Mitochondria, Oxidants, and Aging. Cell 2005, 120, 483-495
    • (2005) Cell , vol.120 , pp. 483-495
    • Balaban, R.S.1    Nemoto, S.2    Finkel, T.3
  • 53
    • 33646678212 scopus 로고    scopus 로고
    • The three-dlmensional structure of complex i from yarrowia lipolytica. A highly dynamic enzyme
    • Radermacher, M.; Ruiz, T.; Clason, T.; Benjamin, S.; Brandt, U.; Zlckermann, V. The Three-Dlmensional Structure of Complex I from Yarrowia lipolytica. A Highly Dynamic Enzyme. J. Struct. Biol. 2006, 154, 269-279.
    • (2006) J. Struct. Biol. , vol.154 , pp. 269-279
    • Radermacher, M.1    Ruiz, T.2    Clason, T.3    Benjamin, S.4    Brandt, U.5    Zlckermann, V.6
  • 54
    • 0032490089 scopus 로고    scopus 로고
    • Iron-sulfur clusters/semiqulnones in complex I
    • Ohnishi, T. Iron-Sulfur Clusters/Semiqulnones in Complex I. Biochim. Biophys. Acta 1998, 1364, 186-206.
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 186-206
    • Ohnishi, T.1
  • 55
    • 33644872938 scopus 로고    scopus 로고
    • Structure of the hydrophilic domain of respiratory complex I from thermus thermophilus
    • Sazanov, L.; Hinchliffo, P. Structure of the Hydrophilic Domain of Respiratory Complex I from Thermus thermophilus. Science 2006, 311, 1430-14306.
    • (2006) Science , vol.311 , pp. 1430-14306
    • Sazanov, L.1    Hinchliffo, P.2
  • 56
    • 34547917597 scopus 로고    scopus 로고
    • Reevaluating the relationship between EPR spectra and enzyme structure for the iron-sulfur clusters in NADH:quinone oxidoreductase
    • DOI 10.1073/pnas.0705593104
    • Yakovlev, G.; Reda, T.; Hirst, J. Reevaluating the Relationship between EPR Spectra and Enzyme Structure for the Iron-Sulfur Clusters in NADH:Qulnone Oxidoreductase. Proc. Natl. Acad. Sci. U.S.A. 2007, 104, 12720-12725. (Pubitemid 47255221)
    • (2007) Proceedings of the National Academy of Sciences of the United States of America , vol.104 , Issue.31 , pp. 12720-12725
    • Yakovlev, G.1    Reda, T.2    Hirst, J.3
  • 59
    • 0031033436 scopus 로고    scopus 로고
    • Proton-translocation by membrane-bound NADH:ubiquinone-oxidoreductase (complex I) through redox-gated ligand conduction
    • DOI 10.1016/S0005-2728(96)00141-7, PII S0005272896001417
    • Brandt, U. Proten-Translocation by Membrane-Bound NADH: UbiqulnoneOxidoreductase (Complex I) through Redox-Gated Ligand Conduction. Biochim. Biophys. Acta 1997, 1318, 79-91. (Pubitemid 27051224)
    • (1997) Biochimica et Biophysica Acta - Bioenergetics , vol.1318 , Issue.1-2 , pp. 79-91
    • Brandt, U.1
  • 60
    • 0142149098 scopus 로고    scopus 로고
    • Two aspartic acid residues in the PSST-homologous NUKM subunit of complex i from yarrowia lipolytica are essential for catalytic activity
    • DOI 10.1074/jbc.M305819200
    • Garofano, A.; Zwicker, K.; Kerscher, S.; Okun, P.; Brandt, U. Two Aspartic Acid Residues in the PSST-Homologous NUKM Subunit of Complex I from Yarrowia lipolytica Arc Essential for Catalytic Activity. J. BmI. Chem. 2003, 278, 4243542440. (Pubitemid 37310515)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.43 , pp. 42435-42440
    • Garofano, A.1    Zwicker, K.2    Kerscher, S.3    Okun, P.4    Brandt, U.5
  • 61
    • 0026530174 scopus 로고
    • Oxygen activation and the conservation of energy in cell respiration
    • Babcock, G. T.; Wlkström, M. Oxygen Activation and the Conservation of Energy in Cell Respiration. Nature 1992, 356, 301-309.
    • (1992) Nature , vol.356 , pp. 301-309
    • Babcock, G.T.1    Wlkström, M.2
  • 63
    • 0028890031 scopus 로고
    • Structure at 2.8 å resolution of cytochrome c oxidase from paracoccus denitriticans
    • Iwata, J.; Ostormoior, C.; Ludwig, B.; Michel, H. Structure at 2.8 Å Resolution of Cytochrome c Oxidase from Paracoccus denitriticans. Nature 1995, 376, 660-669.
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, J.1    Ostormoior, C.2    Ludwig, B.3    Michel, H.4
  • 65
    • 77249104804 scopus 로고    scopus 로고
    • Interaction of cytochrome c with cytochrome c oxidase: Two different docking scenarios
    • Maneg, O.; Malatesa, F.; Ludwig, B.; Drosoii, V. Interaction of Cytochrome c with Cytochrome c Oxidase: Two Different Docking Scenarios. Biochim. Biophys. Acta 2004, 7655, 247-281.
    • (2004) Biochim. Biophys. Acta , vol.7655 , pp. 247-281
    • Maneg, O.1    Malatesa, F.2    Ludwig, B.3    Drosoii, V.4
  • 67
    • 34248139696 scopus 로고    scopus 로고
    • Protein-protein interaction studied by EPR relaxation measurements: Cytochrome c and cytochrome c oxidase
    • Lyubenova, S.; Slddiqul, K.; Penning de Vries, M. J.; Ludwig, B.; Prisner, T. F. Protein-Protein Interaction Studied by EPR Relaxation Measurements: Cytochrome c and Cytochrome c Oxidase. J. Phys. Chem. B 2007, 111, 3839-3846.
    • (2007) J. Phys. Chem. B , vol.111 , pp. 3839-3846
    • Lyubenova, S.1    Slddiqul, K.2    De Vries Penning, M.J.3    Ludwig, B.4    Prisner, T.F.5
  • 68
    • 27944460932 scopus 로고    scopus 로고
    • A structural model for the adduct between cytochrome c and cytochrome c oxidase
    • DOI 10.1007/s00775-005-0011-7
    • Bertini, L.; Cavallaro, G.; Rosato, A. A Structural Model tor the Adduct between Cytochrome c and Cytochrome c Oxidase. J. Biol. Inorg. Chem. 2005, 70, 613-624. (Pubitemid 41673373)
    • (2005) Journal of Biological Inorganic Chemistry , vol.10 , Issue.6 , pp. 613-624
    • Bertini, I.1    Cavallaro, G.2    Rosato, A.3


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