메뉴 건너뛰기




Volumn 437, Issue , 2008, Pages 287-310

The Power of Using Continuous-Wave and Pulsed Electron Paramagnetic Resonance Methods for the Structure Analysis of Ferric Forms and Nitric Oxide-Ligated Ferrous Forms of Globins

Author keywords

[No Author keywords available]

Indexed keywords

CRYSTAL STRUCTURE; ELECTRON SPIN RESONANCE; GEOMETRY; INFORMATION; METHODOLOGY; MICROWAVE RADIATION; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; REVIEW; SPIN LABELING; STRUCTURE ANALYSIS; TECHNOLOGY; ANIMAL; BIOLOGICAL MODEL; CHEMISTRY; EVALUATION; HUMAN; METABOLISM; PROTEIN BINDING; STAINING;

EID: 47049087183     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(07)37015-8     Document Type: Chapter
Times cited : (9)

References (91)
  • 1
    • 0032538786 scopus 로고    scopus 로고
    • On the origin of the low-spin character of cytochrome P450(cam) in the resting state: Investigations of enzyme models with pulse EPR and ENDOR spectroscopy
    • Aissaoui H., Bachmann R., Schweiger A., and Woggon W.D. On the origin of the low-spin character of cytochrome P450(cam) in the resting state: Investigations of enzyme models with pulse EPR and ENDOR spectroscopy. Angew. Chem. Int. Ed. 37 (1998) 2998-3002
    • (1998) Angew. Chem. Int. Ed. , vol.37 , pp. 2998-3002
    • Aissaoui, H.1    Bachmann, R.2    Schweiger, A.3    Woggon, W.D.4
  • 2
    • 0002159495 scopus 로고    scopus 로고
    • Two- and four-pulse ESEEM studies of the heme binding center of a low-spin ferriheme protein: The importance of a multi-frequency approach
    • Astashkin A.V., Raitsimring A.M., and Walker F.A. Two- and four-pulse ESEEM studies of the heme binding center of a low-spin ferriheme protein: The importance of a multi-frequency approach. Chem. Phys. Lett. 306 (1999) 9-17
    • (1999) Chem. Phys. Lett. , vol.306 , pp. 9-17
    • Astashkin, A.V.1    Raitsimring, A.M.2    Walker, F.A.3
  • 3
    • 0031281450 scopus 로고    scopus 로고
    • Contribution of electron paramagnetic resonance to the studies of hemoglobin: The nitrosylhemoglobin system
    • Bemski G. Contribution of electron paramagnetic resonance to the studies of hemoglobin: The nitrosylhemoglobin system. Mol. Biol. Rep. 24 (1997) 263-269
    • (1997) Mol. Biol. Rep. , vol.24 , pp. 263-269
    • Bemski, G.1
  • 4
    • 24344485526 scopus 로고    scopus 로고
    • New developments in high field electron paramagnetic resonance with applications in structural biology
    • Bennati M., and Prisner T.F. New developments in high field electron paramagnetic resonance with applications in structural biology. Rep. Prog. Phys. 68 (2005) 411-448
    • (2005) Rep. Prog. Phys. , vol.68 , pp. 411-448
    • Bennati, M.1    Prisner, T.F.2
  • 5
    • 0348222027 scopus 로고    scopus 로고
    • A continuous-wave and pulsed electron spin resonance spectrometer operating at 275 GHz
    • Block H., Disselhorst J.A.H.M., Orlinskii S.B., and Schmidt J. A continuous-wave and pulsed electron spin resonance spectrometer operating at 275 GHz. J. Magn. Reson. 166 (2004) 92-99
    • (2004) J. Magn. Reson. , vol.166 , pp. 92-99
    • Block, H.1    Disselhorst, J.A.H.M.2    Orlinskii, S.B.3    Schmidt, J.4
  • 6
    • 0000382264 scopus 로고
    • A unified theory for low spin forms of all ferric heme proteins as studied by EPR
    • Chance B., Yonetani T., and Mildvan A.S. (Eds), Academic Press, New York
    • Blumberg W.E., and Peisach J. A unified theory for low spin forms of all ferric heme proteins as studied by EPR. In: Chance B., Yonetani T., and Mildvan A.S. (Eds). "Probes of Structure and Function of Macromolecules and Membranes" Vol. 2 (1971), Academic Press, New York 215
    • (1971) "Probes of Structure and Function of Macromolecules and Membranes" , vol.2 , pp. 215
    • Blumberg, W.E.1    Peisach, J.2
  • 7
    • 0014429411 scopus 로고
    • The electronic structure of protoheme proteins. I. An electron paramagnetic resonance and optical study of horseradish peroxidase and its derivatives
    • Blumberg W.E., Peisach J., Wittenberg B.A., and Wittenberg J.B. The electronic structure of protoheme proteins. I. An electron paramagnetic resonance and optical study of horseradish peroxidase and its derivatives. J. Biol. Chem. 243 (1968) 1854-1862
    • (1968) J. Biol. Chem. , vol.243 , pp. 1854-1862
    • Blumberg, W.E.1    Peisach, J.2    Wittenberg, B.A.3    Wittenberg, J.B.4
  • 8
    • 0035312317 scopus 로고    scopus 로고
    • Nitric oxide moves myoglobin centre stage
    • Brunori M. Nitric oxide moves myoglobin centre stage. Trends Biochem. Sci. 26 (2001) 209-210
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 209-210
    • Brunori, M.1
  • 10
    • 0001743277 scopus 로고
    • A new pulse ENDOR technique
    • Davies E.R. A new pulse ENDOR technique. Phys. Lett. 74A (1974) 1-2
    • (1974) Phys. Lett. , vol.74 A , pp. 1-2
    • Davies, E.R.1
  • 11
    • 0035951095 scopus 로고    scopus 로고
    • EPR-detected folding kinetics of externally located cysteine-directed spin-labeled mutants of iso-1-cytochrome c
    • De Weerd K., Gigoryants V., Sun Y., Fetrow J.S., and Scholes C.P. EPR-detected folding kinetics of externally located cysteine-directed spin-labeled mutants of iso-1-cytochrome c. Biochemistry 40 (2001) 15846-15855
    • (2001) Biochemistry , vol.40 , pp. 15846-15855
    • De Weerd, K.1    Gigoryants, V.2    Sun, Y.3    Fetrow, J.S.4    Scholes, C.P.5
  • 12
    • 0009907828 scopus 로고
    • Electron spin resonance of haemoglobin and myoglobin
    • Dickinson L.C., and Symons M.C.R. Electron spin resonance of haemoglobin and myoglobin. Chem. Soc. Rev. 12 (1983) 387-414
    • (1983) Chem. Soc. Rev. , vol.12 , pp. 387-414
    • Dickinson, L.C.1    Symons, M.C.R.2
  • 14
    • 0000674986 scopus 로고    scopus 로고
    • Electron paramagnetic resonance and electron nuclear double resonance spectroscopy of a heme protein maquette
    • Fahnenschmidt M., Bittl R., Rau H.K., Haehnel W., and Lubitz W. Electron paramagnetic resonance and electron nuclear double resonance spectroscopy of a heme protein maquette. Chem. Phys. Lett. 323 (2000) 329-339
    • (2000) Chem. Phys. Lett. , vol.323 , pp. 329-339
    • Fahnenschmidt, M.1    Bittl, R.2    Rau, H.K.3    Haehnel, W.4    Lubitz, W.5
  • 15
    • 0028066239 scopus 로고
    • ENDOR determination of heme ligation in chloroperoxidase and comparison with cytochrome P450cam
    • Fann Y.C., Gerber N.C., Osmulski P.A., Hager L.P., Sligar S.G., and Hoffman B.M. ENDOR determination of heme ligation in chloroperoxidase and comparison with cytochrome P450cam. J. Am. Chem. Soc. 116 (1994) 5989-5990
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 5989-5990
    • Fann, Y.C.1    Gerber, N.C.2    Osmulski, P.A.3    Hager, L.P.4    Sligar, S.G.5    Hoffman, B.M.6
  • 16
    • 0000237476 scopus 로고
    • 1,2H ENDOR study of distal-pocket N(ε{lunate})-H...F hydrogen bonding in fluorometmyoglobin
    • 1,2H ENDOR study of distal-pocket N(ε{lunate})-H...F hydrogen bonding in fluorometmyoglobin. J. Am. Chem. Soc. 117 (1995) 6109-6116
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 6109-6116
    • Fann, Y.1    Ong, J.2    Nocek, J.M.3    Hoffman, B.M.4
  • 17
    • 36149020457 scopus 로고
    • Observation of nuclear magnetic resonances via the electron spin resonance line
    • Feher G. Observation of nuclear magnetic resonances via the electron spin resonance line. Phys. Rev. 103 (1959) 834-835
    • (1959) Phys. Rev. , vol.103 , pp. 834-835
    • Feher, G.1
  • 18
    • 0030819745 scopus 로고    scopus 로고
    • Temperature dependence of Q-band electron paramagnetic resonance spectra of nitrosyl heme proteins
    • Flores M., Wajnberg E., and Bemski G. Temperature dependence of Q-band electron paramagnetic resonance spectra of nitrosyl heme proteins. Biophys. J. 73 (1997) 3225-3229
    • (1997) Biophys. J. , vol.73 , pp. 3225-3229
    • Flores, M.1    Wajnberg, E.2    Bemski, G.3
  • 19
    • 0034034777 scopus 로고    scopus 로고
    • Proton electron nuclear double resonance from nitrosyl horse heart myoglobin: The role of His-E7 and Val-E11
    • Flores M., Wajnberg E., and Bemski G. Proton electron nuclear double resonance from nitrosyl horse heart myoglobin: The role of His-E7 and Val-E11. Biophys. J. 78 (2000) 2107-2115
    • (2000) Biophys. J. , vol.78 , pp. 2107-2115
    • Flores, M.1    Wajnberg, E.2    Bemski, G.3
  • 20
    • 0033660661 scopus 로고    scopus 로고
    • New technologies in electron spin resonance
    • Freed J.H. New technologies in electron spin resonance. Annu. Rev. Phys. Chem. 51 (2000) 655-689
    • (2000) Annu. Rev. Phys. Chem. , vol.51 , pp. 655-689
    • Freed, J.H.1
  • 21
    • 10444268100 scopus 로고    scopus 로고
    • Globin-coupled sensors, protoglobins, and the last universal common ancestor
    • Freitas T.A.K., Saito J.A., Hou S., and Alam M. Globin-coupled sensors, protoglobins, and the last universal common ancestor. J. Inorg. Biochem. 99 (2005) 23-33
    • (2005) J. Inorg. Biochem. , vol.99 , pp. 23-33
    • Freitas, T.A.K.1    Saito, J.A.2    Hou, S.3    Alam, M.4
  • 22
    • 0141783647 scopus 로고    scopus 로고
    • Bacterial hemoglobins and flavohemoglobins: Versatile proteins and their impact on microbiology and biotechnology
    • Frey A.D., and Kallio P.T. Bacterial hemoglobins and flavohemoglobins: Versatile proteins and their impact on microbiology and biotechnology. FEMS Microbiol. Rev. 27 (2003) 525-545
    • (2003) FEMS Microbiol. Rev. , vol.27 , pp. 525-545
    • Frey, A.D.1    Kallio, P.T.2
  • 25
    • 0035400133 scopus 로고    scopus 로고
    • 14N symmetry about the Fe-NO plane: A hyperfine sublevel correlation spectroscopy study
    • 14N symmetry about the Fe-NO plane: A hyperfine sublevel correlation spectroscopy study. Chem. Phys. 269 (2001) 125-135
    • (2001) Chem. Phys. , vol.269 , pp. 125-135
    • Gilbert, D.C.1    Doetschman, D.C.2
  • 26
    • 33746429668 scopus 로고    scopus 로고
    • High field ENDOR as a characterization tool for functional sites in microporous materials
    • Goldfarb D. High field ENDOR as a characterization tool for functional sites in microporous materials. Phys. Chem. Chem. Phys. 8 (2006) 2325-2343
    • (2006) Phys. Chem. Chem. Phys. , vol.8 , pp. 2325-2343
    • Goldfarb, D.1
  • 27
    • 0000242143 scopus 로고
    • Hyperfine sublevel correlation (HYSCORE) spectroscopy: A 2D ESR investigation of the squaric acid radical
    • Höfer P., Grupp A., Nebenführ H., and Mehring M. Hyperfine sublevel correlation (HYSCORE) spectroscopy: A 2D ESR investigation of the squaric acid radical. Chem. Phys. Lett. 132 (1986) 279-282
    • (1986) Chem. Phys. Lett. , vol.132 , pp. 279-282
    • Höfer, P.1    Grupp, A.2    Nebenführ, H.3    Mehring, M.4
  • 29
    • 0033741861 scopus 로고    scopus 로고
    • EPR studies on the photoinduced intermediates of NO complexes in recombinant ferric Mb trapped at low temperature
    • Hori H., Masuya F., Dou Y., and Ikeda-Saito M. EPR studies on the photoinduced intermediates of NO complexes in recombinant ferric Mb trapped at low temperature. J. Inorg. Biochem. 82 (2000) 181-187
    • (2000) J. Inorg. Biochem. , vol.82 , pp. 181-187
    • Hori, H.1    Masuya, F.2    Dou, Y.3    Ikeda-Saito, M.4
  • 30
    • 0033812585 scopus 로고    scopus 로고
    • Identifying conformational changes with site-directed spin labeling
    • Hubbell W.L., Cafiso D.S., and Altenbach C. Identifying conformational changes with site-directed spin labeling. Nat. Struct. Mol. Biol. 7 (2000) 735-739
    • (2000) Nat. Struct. Mol. Biol. , vol.7 , pp. 735-739
    • Hubbell, W.L.1    Cafiso, D.S.2    Altenbach, C.3
  • 31
    • 0000779687 scopus 로고
    • Proton ENDOR from randomly oriented NO-ligated hemoglobin: Approaching the structural basis for the R-T transition
    • Hüttermann J., Burgard C., and Kappl R. Proton ENDOR from randomly oriented NO-ligated hemoglobin: Approaching the structural basis for the R-T transition. J. Chem. Soc. Faraday Trans. 90 (1994) 3077-3087
    • (1994) J. Chem. Soc. Faraday Trans. , vol.90 , pp. 3077-3087
    • Hüttermann, J.1    Burgard, C.2    Kappl, R.3
  • 34
    • 0037112592 scopus 로고    scopus 로고
    • Distance measurements in the nanometer range by pulse EPR
    • Jeschke G. Distance measurements in the nanometer range by pulse EPR. Chem. Phys. Chem. 3 (2002) 927-932
    • (2002) Chem. Phys. Chem. , vol.3 , pp. 927-932
    • Jeschke, G.1
  • 35
    • 0001671730 scopus 로고    scopus 로고
    • Sensitivity enhancement by matched microwave pulses in one- and two-dimensional electron spin echo envelope modulation spectroscopy
    • Jeschke G., Rakhmatullin R., and Schweiger A. Sensitivity enhancement by matched microwave pulses in one- and two-dimensional electron spin echo envelope modulation spectroscopy. J. Magn. Reson. 131 (1998) 261-271
    • (1998) J. Magn. Reson. , vol.131 , pp. 261-271
    • Jeschke, G.1    Rakhmatullin, R.2    Schweiger, A.3
  • 36
    • 0000610025 scopus 로고
    • Hyperfine-correlated electron nuclear double resonance spectroscopy
    • Jeschke G., and Schweiger A. Hyperfine-correlated electron nuclear double resonance spectroscopy. Chem. Phys. Lett. 246 (1995) 431-438
    • (1995) Chem. Phys. Lett. , vol.246 , pp. 431-438
    • Jeschke, G.1    Schweiger, A.2
  • 37
    • 0004740720 scopus 로고    scopus 로고
    • NMR-correlated high-field electron paramagnetic resonance spectroscopy
    • Jeschke G., and Spiess H.W. NMR-correlated high-field electron paramagnetic resonance spectroscopy. Chem. Phys. Lett. 293 (1998) 9-18
    • (1998) Chem. Phys. Lett. , vol.293 , pp. 9-18
    • Jeschke, G.1    Spiess, H.W.2
  • 39
    • 85005481091 scopus 로고
    • An ENDOR study of nitrosyl myoglobin single crystals
    • Kappl R., and Hütterman J. An ENDOR study of nitrosyl myoglobin single crystals. Isr. J. Chem. 29 (1989) 73-84
    • (1989) Isr. J. Chem. , vol.29 , pp. 73-84
    • Kappl, R.1    Hütterman, J.2
  • 40
    • 3042640517 scopus 로고    scopus 로고
    • Kaupp M., Bühl M., and Malkin V.G. (Eds), Wiley-VCH, Weinheim
    • In: Kaupp M., Bühl M., and Malkin V.G. (Eds). "Calculations of NMR and EPR parameters." (2004), Wiley-VCH, Weinheim
    • (2004) "Calculations of NMR and EPR parameters."
  • 42
    • 0038203083 scopus 로고    scopus 로고
    • A two-faced molecule offers NO explanation: The proximal binding of nitric oxide to haem
    • Lawson D.M., Stevenson C.E.M., Andrew C.R., George S.J., and Eady R.R. A two-faced molecule offers NO explanation: The proximal binding of nitric oxide to haem. Biochem. Soc. Trans. 31 (2003) 553-557
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 553-557
    • Lawson, D.M.1    Stevenson, C.E.M.2    Andrew, C.R.3    George, S.J.4    Eady, R.R.5
  • 43
    • 0030908542 scopus 로고    scopus 로고
    • Structure of the modified heme in allylbenzene-inactivated chloroperoxidase determined by Q-band CW and pulsed ENDOR
    • Lee H.I., Dexter A.F., Fann Y.C., Lakner F.J., Hager L.P., and Hoffman B.M. Structure of the modified heme in allylbenzene-inactivated chloroperoxidase determined by Q-band CW and pulsed ENDOR. J. Am. Chem. Soc. 119 (1997) 4059-4069
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 4059-4069
    • Lee, H.I.1    Dexter, A.F.2    Fann, Y.C.3    Lakner, F.J.4    Hager, L.P.5    Hoffman, B.M.6
  • 44
    • 0035367368 scopus 로고    scopus 로고
    • Multiple quantum coherence in HYSCORE spectra
    • Liesum L., and Schweiger A. Multiple quantum coherence in HYSCORE spectra. J. Chem. Phys. 114 (2001) 9478-9488
    • (2001) J. Chem. Phys. , vol.114 , pp. 9478-9488
    • Liesum, L.1    Schweiger, A.2
  • 46
    • 0021377727 scopus 로고
    • Electron paramagnetic resonance- (EPR-) resolved kinetics of cryogenic nitric oxide recombination to cytochrome c oxidase and myoglobin
    • LoBrutto R., Wei Y.H., Yoshida S., Van Camp H.L., Scholes C.P., and King T.E. Electron paramagnetic resonance- (EPR-) resolved kinetics of cryogenic nitric oxide recombination to cytochrome c oxidase and myoglobin. Biophys. J. 45 (1984) 473-479
    • (1984) Biophys. J. , vol.45 , pp. 473-479
    • LoBrutto, R.1    Wei, Y.H.2    Yoshida, S.3    Van Camp, H.L.4    Scholes, C.P.5    King, T.E.6
  • 47
    • 0542431396 scopus 로고
    • Electric field effects in spin echoes
    • Mims W.B. Electric field effects in spin echoes. Phys. Rev. 133 (1964) A835-A840
    • (1964) Phys. Rev. , vol.133
    • Mims, W.B.1
  • 48
    • 0000465369 scopus 로고
    • Pulsed ENDOR experiments
    • Mims W.B. Pulsed ENDOR experiments. Proc. R. Soc. Lond. 283 (1965) 452-457
    • (1965) Proc. R. Soc. Lond. , vol.283 , pp. 452-457
    • Mims, W.B.1
  • 49
    • 12444328805 scopus 로고    scopus 로고
    • High-field EPR spectroscopy applied to biological systems: Characterization of molecular switches for electron and ion transfer
    • Möbius K., Savitsky A., Schnegg A., Plato M., and Fuchs M. High-field EPR spectroscopy applied to biological systems: Characterization of molecular switches for electron and ion transfer. Phys. Chem. Chem. Phys. 7 (2005) 19-42
    • (2005) Phys. Chem. Chem. Phys. , vol.7 , pp. 19-42
    • Möbius, K.1    Savitsky, A.2    Schnegg, A.3    Plato, M.4    Fuchs, M.5
  • 50
    • 0019127299 scopus 로고
    • Electron paramagnetic resonance studies of nitrosyl ferrous heme complexes: Determination of an equilibrium between two conformations
    • Morse R.H., and Chan S.I. Electron paramagnetic resonance studies of nitrosyl ferrous heme complexes: Determination of an equilibrium between two conformations. J. Biol. Chem. 255 (1980) 7876-7882
    • (1980) J. Biol. Chem. , vol.255 , pp. 7876-7882
    • Morse, R.H.1    Chan, S.I.2
  • 51
    • 84966781578 scopus 로고    scopus 로고
    • Interpretation and calculation of spin-Hamiltonian parameters in transition metal complexes
    • Miller J.S., and Drillon M. (Eds), Wiley-VCH, Weinheim
    • Neese F., and Solomon E.I. Interpretation and calculation of spin-Hamiltonian parameters in transition metal complexes. In: Miller J.S., and Drillon M. (Eds). "Magnetism: Molecules to Materials IV" (2003), Wiley-VCH, Weinheim 345-466
    • (2003) "Magnetism: Molecules to Materials IV" , pp. 345-466
    • Neese, F.1    Solomon, E.I.2
  • 52
    • 0003791868 scopus 로고    scopus 로고
    • Packer L. (Ed), Academic Press, San Diego
    • In: Packer L. (Ed). "Methods in Enzymology," Vol. 269 (1996), Academic Press, San Diego
    • (1996) "Methods in Enzymology," , vol.269
  • 53
    • 0034645113 scopus 로고    scopus 로고
    • Structural origin of two paramagnetic species in six-coordinated nitrosoiron(II) porphyrins revealed by density functional theory Analysis of the g tensors
    • Patchkovskii S., and Ziegler T. Structural origin of two paramagnetic species in six-coordinated nitrosoiron(II) porphyrins revealed by density functional theory Analysis of the g tensors. Inorg. Chem. 39 (2000) 5354-5364
    • (2000) Inorg. Chem. , vol.39 , pp. 5354-5364
    • Patchkovskii, S.1    Ziegler, T.2
  • 54
    • 0018801615 scopus 로고
    • 14N in cytochrome P450 and in a series of low spin heme compounds
    • 14N in cytochrome P450 and in a series of low spin heme compounds. J. Biol. Chem. 254 (1979) 12379-12389
    • (1979) J. Biol. Chem. , vol.254 , pp. 12379-12389
    • Peisach, J.1    Mims, W.B.2    Davis, J.L.3
  • 55
    • 0018654083 scopus 로고
    • Regulation of oxygen affinity of hemoglobin: Influence of structure of the globin on the heme iron
    • Perutz M. Regulation of oxygen affinity of hemoglobin: Influence of structure of the globin on the heme iron. Annu. Rev. Biochem. 48 (1979) 327-386
    • (1979) Annu. Rev. Biochem. , vol.48 , pp. 327-386
    • Perutz, M.1
  • 57
  • 58
    • 28844476036 scopus 로고    scopus 로고
    • Electron paramagnetic resonance analysis of nitrosylhemoglobin in humans during NO inhalation
    • Piknova B., Gladwin M.T., Schechter A.N., and Hogg N. Electron paramagnetic resonance analysis of nitrosylhemoglobin in humans during NO inhalation. J. Biol. Chem. 280 (2005) 40583-40588
    • (2005) J. Biol. Chem. , vol.280 , pp. 40583-40588
    • Piknova, B.1    Gladwin, M.T.2    Schechter, A.N.3    Hogg, N.4
  • 59
    • 0030937861 scopus 로고    scopus 로고
    • Kinetics and motional dynamics of spin-labeled yeast iso-1-cytochrome c. 1. Stopped-flow electron paramagnetic resonance as a probe for protein folding/unfolding of the C-terminal helix spin-labeled at cysteine 102
    • Qu K., Vaughn L., Sienkiewicz A., Scholes C.P., and Fetrow J.S. Kinetics and motional dynamics of spin-labeled yeast iso-1-cytochrome c. 1. Stopped-flow electron paramagnetic resonance as a probe for protein folding/unfolding of the C-terminal helix spin-labeled at cysteine 102. Biochemistry 36 (1997) 2884-2897
    • (1997) Biochemistry , vol.36 , pp. 2884-2897
    • Qu, K.1    Vaughn, L.2    Sienkiewicz, A.3    Scholes, C.P.4    Fetrow, J.S.5
  • 60
    • 0000964520 scopus 로고
    • Electronic structure of low-spin ferric porphyrins: A single-crystal EPR and structural investigation of the influence of axial ligand orientation and the effects of pseudo-Jahn-Teller distortion
    • Quinn R., Valentine J.S., Byrn M.P., and Strouse C.E. Electronic structure of low-spin ferric porphyrins: A single-crystal EPR and structural investigation of the influence of axial ligand orientation and the effects of pseudo-Jahn-Teller distortion. J. Am. Chem. Soc. 109 (1987) 3301-3308
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 3301-3308
    • Quinn, R.1    Valentine, J.S.2    Byrn, M.P.3    Strouse, C.E.4
  • 61
    • 0000871923 scopus 로고    scopus 로고
    • Magnetic field (g-value) dependence of proton hyperfine couplings obtained from ESEEM measurements: Determination of the orientation of the magnetic axes of model heme complexes in glassy media
    • Raitsimring A.M., Borbat P., Shokhireva T.K., and Walker F.A. Magnetic field (g-value) dependence of proton hyperfine couplings obtained from ESEEM measurements: Determination of the orientation of the magnetic axes of model heme complexes in glassy media. J. Am. Chem. Soc. 100 (1996) 5235-5244
    • (1996) J. Am. Chem. Soc. , vol.100 , pp. 5235-5244
    • Raitsimring, A.M.1    Borbat, P.2    Shokhireva, T.K.3    Walker, F.A.4
  • 62
    • 0032576122 scopus 로고    scopus 로고
    • Determination of the Fe-ligand bond lengths and Fe-N-O bond angles in horse heart ferric and ferrous nitrosylmyoglobin using multiple-scattering XAFS analyses
    • Rich A.M., Armstrong R.S., Ellis P.J., and Lay P.A. Determination of the Fe-ligand bond lengths and Fe-N-O bond angles in horse heart ferric and ferrous nitrosylmyoglobin using multiple-scattering XAFS analyses. J. Am. Chem. Soc. 120 (1998) 10827-10836
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 10827-10836
    • Rich, A.M.1    Armstrong, R.S.2    Ellis, P.J.3    Lay, P.A.4
  • 63
    • 0035528065 scopus 로고    scopus 로고
    • On the Mode of hexacoordinated NO-Binding to myo- and hemoglobin: Variable-temperature EPR studies at multiple microwave frequencies
    • Schmidt P.P., Kappl R., and Hüttermann J. On the Mode of hexacoordinated NO-Binding to myo- and hemoglobin: Variable-temperature EPR studies at multiple microwave frequencies. Appl. Magn. Reson. 21 (2001) 423-440
    • (2001) Appl. Magn. Reson. , vol.21 , pp. 423-440
    • Schmidt, P.P.1    Kappl, R.2    Hüttermann, J.3
  • 64
    • 0000271496 scopus 로고
    • Electron nuclear double resonance (ENDOR) of bis(imidazole)-ligated low-spin ferric heme systems
    • Scholes C.P., Falkowski K.M., Chen S., and Bank J. Electron nuclear double resonance (ENDOR) of bis(imidazole)-ligated low-spin ferric heme systems. J. Am. Chem. Soc. 108 (1986) 1660-1671
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 1660-1671
    • Scholes, C.P.1    Falkowski, K.M.2    Chen, S.3    Bank, J.4
  • 65
    • 0001428732 scopus 로고
    • Electron nuclear double resonance (ENDOR) from heme and histidine nitrogens in single crystals of aquometmyoglobin
    • Scholes C.P., Lapidot A., Mascarenhas R., Inubushi T., Isaacson R.A., and Feher G. Electron nuclear double resonance (ENDOR) from heme and histidine nitrogens in single crystals of aquometmyoglobin. J. Am. Chem. Soc. 104 (1982) 2724-2735
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 2724-2735
    • Scholes, C.P.1    Lapidot, A.2    Mascarenhas, R.3    Inubushi, T.4    Isaacson, R.A.5    Feher, G.6
  • 66
    • 33748244205 scopus 로고
    • Pulsed electron spin resonance spectroscopy: Basic principles, techniques, and examples of applications
    • Schweiger A. Pulsed electron spin resonance spectroscopy: Basic principles, techniques, and examples of applications. Angew. Chem. Int. Ed. Engl. 30 (1991) 265-292
    • (1991) Angew. Chem. Int. Ed. Engl. , vol.30 , pp. 265-292
    • Schweiger, A.1
  • 68
    • 0009955072 scopus 로고
    • ESR of iron proteins
    • Berliner L.J., and Reuben J. (Eds), Plenum, New York
    • Smith D.T., and Pilbrow J.R. ESR of iron proteins. In: Berliner L.J., and Reuben J. (Eds). "Biological Magnetic Resonance" Vol. 2 (1980), Plenum, New York 85
    • (1980) "Biological Magnetic Resonance" , vol.2 , pp. 85
    • Smith, D.T.1    Pilbrow, J.R.2
  • 70
    • 0017593566 scopus 로고
    • 2g hole model to the directional properties of the g tensor, and a new method for calculating the ligand field parameters
    • 2g hole model to the directional properties of the g tensor, and a new method for calculating the ligand field parameters. Biochim. Biophys. Acta 491 (1977) 139-148
    • (1977) Biochim. Biophys. Acta , vol.491 , pp. 139-148
    • Taylor, C.P.S.1
  • 71
    • 34249068326 scopus 로고    scopus 로고
    • Studying high-spin ferric heme proteins using pulsed EPR spectroscopy: Analysis of the ferric form of the E7Q mutant of human neuroglobin
    • Trandafir F., ter Heerdt P., Fittipaldi M., Vinck E., Dewilde S., Moens L., and Van Doorslaer S. Studying high-spin ferric heme proteins using pulsed EPR spectroscopy: Analysis of the ferric form of the E7Q mutant of human neuroglobin. Appl. Magn. Reson. 31 (2007) 553-572
    • (2007) Appl. Magn. Reson. , vol.31 , pp. 553-572
    • Trandafir, F.1    ter Heerdt, P.2    Fittipaldi, M.3    Vinck, E.4    Dewilde, S.5    Moens, L.6    Van Doorslaer, S.7
  • 73
    • 0033553147 scopus 로고    scopus 로고
    • Characterization of bimodal coordination structure in nitrosyl heme complexes through hyperfine couplings with pyrrole and protein nitrogens
    • Tyryshkin A.M., Dikanov S.A., Reijerse E.J., Burgard C., and Hüttermann J. Characterization of bimodal coordination structure in nitrosyl heme complexes through hyperfine couplings with pyrrole and protein nitrogens. J. Am. Chem. Soc. 121 (1999) 3396-3406
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 3396-3406
    • Tyryshkin, A.M.1    Dikanov, S.A.2    Reijerse, E.J.3    Burgard, C.4    Hüttermann, J.5
  • 75
    • 36749114016 scopus 로고
    • EPR study of the structure and spin distribution at the binding site in human nitrosylhemoglobin single crystals
    • Utterback S.G., Doetschman D.C., Szumowski J., and Rizos A.K. EPR study of the structure and spin distribution at the binding site in human nitrosylhemoglobin single crystals. J. Chem. Phys. 78 (1983) 5874-5880
    • (1983) J. Chem. Phys. , vol.78 , pp. 5874-5880
    • Utterback, S.G.1    Doetschman, D.C.2    Szumowski, J.3    Rizos, A.K.4
  • 76
    • 0017300680 scopus 로고
    • Electron nuclear double resonance on heme compounds: ENDOR from the iron ligands in protohemin chloride and protohemin bromide
    • Van Camp H.L., Scholes C.P., and Mulks C.F. Electron nuclear double resonance on heme compounds: ENDOR from the iron ligands in protohemin chloride and protohemin bromide. J. Am. Chem. Soc. 98 (1976) 4094-4098
    • (1976) J. Am. Chem. Soc. , vol.98 , pp. 4094-4098
    • Van Camp, H.L.1    Scholes, C.P.2    Mulks, C.F.3
  • 77
    • 52049115704 scopus 로고    scopus 로고
    • New hyperfine-decoupling schemes in electron paramagnetic resonance spectroscopy
    • Van Doorslaer S., and Schweiger A. New hyperfine-decoupling schemes in electron paramagnetic resonance spectroscopy. Chem. Phys. Lett. 281 (1999) 297-305
    • (1999) Chem. Phys. Lett. , vol.281 , pp. 297-305
    • Van Doorslaer, S.1    Schweiger, A.2
  • 78
    • 33748647979 scopus 로고    scopus 로고
    • Multi-frequency EPR spectroscopy of myoglobin: Spectral effects for high-spin iron(III) ion at high magnetic fields
    • van Kan P.J.M., van der Horst E., Reijerse E.J., van Bentum P.J.M., and Hagen W.R. Multi-frequency EPR spectroscopy of myoglobin: Spectral effects for high-spin iron(III) ion at high magnetic fields. J. Chem. Soc. Faraday Trans. 94 (1998) 2975-2978
    • (1998) J. Chem. Soc. Faraday Trans. , vol.94 , pp. 2975-2978
    • van Kan, P.J.M.1    van der Horst, E.2    Reijerse, E.J.3    van Bentum, P.J.M.4    Hagen, W.R.5
  • 79
    • 0034644426 scopus 로고    scopus 로고
    • Q-band ENDOR (electron nuclear double resonance) of the heme o3 liganding environment at the binuclear center in cytochrome bo3 from
    • Veselov A.V., Osborne J.P., Gennis R.B., and Scholes C.P. Q-band ENDOR (electron nuclear double resonance) of the heme o3 liganding environment at the binuclear center in cytochrome bo3 from. Escherichia coli. J. Am. Chem. Soc. 122 (2000) 8712-8716
    • (2000) Escherichia coli. J. Am. Chem. Soc. , vol.122 , pp. 8712-8716
    • Veselov, A.V.1    Osborne, J.P.2    Gennis, R.B.3    Scholes, C.P.4
  • 80
    • 10944262736 scopus 로고    scopus 로고
    • Analysing low-spin ferric complexes using pulse EPR techniques: A structure determination of bis(4-methylimidazole)(tetraphenylporphyrinato)iron(III)
    • Vinck E., and Van Doorslaer S. Analysing low-spin ferric complexes using pulse EPR techniques: A structure determination of bis(4-methylimidazole)(tetraphenylporphyrinato)iron(III). Phys. Chem. Chem. Phys. 6 (2004) 5324-5330
    • (2004) Phys. Chem. Chem. Phys. , vol.6 , pp. 5324-5330
    • Vinck, E.1    Van Doorslaer, S.2
  • 81
    • 33745760567 scopus 로고    scopus 로고
    • Analyzing heme proteins using EPR techniques: The heme-pocket structure of ferric mouse neuroglobin
    • Vinck E., Van Doorslaer S., Dewilde S., Mitrikas G., Schweiger A., and Moens L. Analyzing heme proteins using EPR techniques: The heme-pocket structure of ferric mouse neuroglobin. J. Biol. Inorg. Chem. 11 (2006) 467-475
    • (2006) J. Biol. Inorg. Chem. , vol.11 , pp. 467-475
    • Vinck, E.1    Van Doorslaer, S.2    Dewilde, S.3    Mitrikas, G.4    Schweiger, A.5    Moens, L.6
  • 82
    • 1842637797 scopus 로고    scopus 로고
    • Structural change of the heme pocket due to disulfide bridge formation is significantly larger for neuroglobin than for cytoglobin
    • Vinck E., Van Doorslaer S., Dewilde S., and Moens L. Structural change of the heme pocket due to disulfide bridge formation is significantly larger for neuroglobin than for cytoglobin. J. Am. Chem. Soc. 126 (2004) 4516-4517
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 4516-4517
    • Vinck, E.1    Van Doorslaer, S.2    Dewilde, S.3    Moens, L.4
  • 83
    • 33845373654 scopus 로고
    • Models of the cytochromes. b. Effect of axial ligand plane orientation on the EPR and Moessbauer spectra of low-spin ferrihemes
    • Walker F.A., Huynh B.H., Scheidt W.R., and Osvath S.R. Models of the cytochromes. b. Effect of axial ligand plane orientation on the EPR and Moessbauer spectra of low-spin ferrihemes. J. Am. Chem. Soc. 108 (1986) 5288-5297
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 5288-5297
    • Walker, F.A.1    Huynh, B.H.2    Scheidt, W.R.3    Osvath, S.R.4
  • 84
    • 0035066385 scopus 로고    scopus 로고
    • Nonvertebrate hemoglobins: Functions and molecular adaptations
    • Weber R.E., and Vinogradov S.N. Nonvertebrate hemoglobins: Functions and molecular adaptations. Physiol. Rev. 81 (2001) 569-628
    • (2001) Physiol. Rev. , vol.81 , pp. 569-628
    • Weber, R.E.1    Vinogradov, S.N.2
  • 86
    • 0025310053 scopus 로고
    • Mechanisms of cytoplasmic hemoglobin and myoglobin function
    • Wittenberg J.B., and Wittenberg B.A. Mechanisms of cytoplasmic hemoglobin and myoglobin function. Annu. Rev. Biophys. Chem. 19 (1990) 217-241
    • (1990) Annu. Rev. Biophys. Chem. , vol.19 , pp. 217-241
    • Wittenberg, J.B.1    Wittenberg, B.A.2
  • 87
    • 0041874993 scopus 로고    scopus 로고
    • Five- to six-coordination in (nitrosyl)iron (II) porphyrinates: Effects of binding the sixth ligand
    • Wyllie G.R.A., Schulz C.E., and Scheidt W.R. Five- to six-coordination in (nitrosyl)iron (II) porphyrinates: Effects of binding the sixth ligand. Inorg. Chem. 42 (2003) 5722-5734
    • (2003) Inorg. Chem. , vol.42 , pp. 5722-5734
    • Wyllie, G.R.A.1    Schulz, C.E.2    Scheidt, W.R.3
  • 88
    • 0032493731 scopus 로고    scopus 로고
    • Electron paramagnetic resonance and oxygen binding studies of alpha-nitrosyl hemoglobin: A novel oxygen carrier having NO-assisted allosteric functions
    • Yonetani T., Tsuneshige A., Zhou Y., and Chen X. Electron paramagnetic resonance and oxygen binding studies of alpha-nitrosyl hemoglobin: A novel oxygen carrier having NO-assisted allosteric functions. J. Biol. Chem. 273 (1998) 20323-20333
    • (1998) J. Biol. Chem. , vol.273 , pp. 20323-20333
    • Yonetani, T.1    Tsuneshige, A.2    Zhou, Y.3    Chen, X.4
  • 89
    • 0015522926 scopus 로고
    • Electromagnetic properties of hemoproteins. V. Optical and electron paramagnetic resonance characteristics of nitric oxide derivatives of metalloporphyrin-apohemoprotein complexes
    • Yonetani T., Yamamoto H., Erman J.E., Leigh Jr. J.S., and Reed G.H. Electromagnetic properties of hemoproteins. V. Optical and electron paramagnetic resonance characteristics of nitric oxide derivatives of metalloporphyrin-apohemoprotein complexes. J. Biol. Chem. 247 (1972) 2447-2455
    • (1972) J. Biol. Chem. , vol.247 , pp. 2447-2455
    • Yonetani, T.1    Yamamoto, H.2    Erman, J.E.3    Leigh Jr., J.S.4    Reed, G.H.5
  • 90
    • 0345802951 scopus 로고    scopus 로고
    • A density functional theory investigation of Fe-N-O bonding in heme proteins and model systems
    • Zhang Y., Gossman W., and Oldfield E. A density functional theory investigation of Fe-N-O bonding in heme proteins and model systems. J. Am. Chem. Soc. 125 (2003) 16387-16396
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 16387-16396
    • Zhang, Y.1    Gossman, W.2    Oldfield, E.3
  • 91
    • 2442546520 scopus 로고    scopus 로고
    • Magnetic and hyperfine properties of deoxymyoglobin and nitrosyl-myoglobin
    • Zhi Z., Guenzburger D., and Ellis D.E. Magnetic and hyperfine properties of deoxymyoglobin and nitrosyl-myoglobin. J. Mol. Struct. THEOCHEM 678 (2004) 145-156
    • (2004) J. Mol. Struct. THEOCHEM , vol.678 , pp. 145-156
    • Zhi, Z.1    Guenzburger, D.2    Ellis, D.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.