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Volumn 78, Issue 4, 2000, Pages 2107-2115

Proton electron nuclear double resonance from nitrosyl horse heart myoglobin: The role of His-E7 and Val-E11

Author keywords

[No Author keywords available]

Indexed keywords

MYOGLOBIN; PROTON;

EID: 0034034777     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(00)76757-9     Document Type: Article
Times cited : (19)

References (51)
  • 3
    • 0004783330 scopus 로고
    • The electron spin distribution in nitrosylhemoglobin
    • Doetschman, D. C., S. A. Schwartz, and S. G. Utterback. 1980. The electron spin distribution in nitrosylhemoglobin. Chem. Phys. 49:1-8.
    • (1980) Chem. Phys. , vol.49 , pp. 1-8
    • Doetschman, D.C.1    Schwartz, S.A.2    Utterback, S.G.3
  • 4
    • 0015693260 scopus 로고
    • Electron nuclear double resonance (ENDOR) investigation on myoglobin and hemoglobin
    • Feher, G., R. A. Isaacson, C. P. Scholes, and R. Nagel. 1973. Electron nuclear double resonance (ENDOR) investigation on myoglobin and hemoglobin. Ann. N.Y. Acad. Sci. 222:86-101.
    • (1973) Ann. N.y. Acad. Sci. , vol.222 , pp. 86-101
    • Feher, G.1    Isaacson, R.A.2    Scholes, C.P.3    Nagel, R.4
  • 5
    • 0030819745 scopus 로고    scopus 로고
    • Temperature dependence of Q-band electron paramagnetic resonance spectra of nitrosyl heme proteins
    • Flores, M., E. Wajnberg, and G. Bemski. 1997. Temperature dependence of Q-band electron paramagnetic resonance spectra of nitrosyl heme proteins. Biophys. J. 73:3225-3229.
    • (1997) Biophys. J. , vol.73 , pp. 3225-3229
    • Flores, M.1    Wajnberg, E.2    Bemski, G.3
  • 6
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • Frauenfelder, H., S. G. Sligar, and P. G. Wolynes. 1991. The energy landscapes and motions of proteins. Science. 254:1598-1603.
    • (1991) Science. , vol.254 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 8
    • 0019888621 scopus 로고
    • Real space refinement of neutron-diffraction data from sperm whale carbonmonoxy-myoglobin
    • Hanson, J. C., and B. P. Schoenborn. 1981. Real space refinement of neutron-diffraction data from sperm whale carbonmonoxy-myoglobin. J. Mol. Bint. 153:117-146.
    • (1981) J. Mol. Bint. , vol.153 , pp. 117-146
    • Hanson, J.C.1    Schoenborn, B.P.2
  • 9
    • 33845376623 scopus 로고
    • Angle-selected ENDOR spectroscopy. 2. Determination of proton coordinates from a polycrystalline sample of bis (2,4-pentanedionato) copper(II)
    • Henderson, T. A., G. C. Hurst, and R. W. Kreilick. 1985. Angle-selected ENDOR spectroscopy. 2. Determination of proton coordinates from a polycrystalline sample of bis (2,4-pentanedionato) copper(II). J. Am. Chem. Soc. 107:7299-7303.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 7299-7303
    • Henderson, T.A.1    Hurst, G.C.2    Kreilick, R.W.3
  • 10
    • 0001091552 scopus 로고
    • Polycrystalline ENDOR patterns from centers with axial EPR spectra. General formulas and simple analytic expressions for deriving geometric information from dipolar coupling
    • Hoffman, B. M., and R. J. Gurbiel. 1989. Polycrystalline ENDOR patterns from centers with axial EPR spectra. General formulas and simple analytic expressions for deriving geometric information from dipolar coupling. J. Magn. Reson. 82:309-317.
    • (1989) J. Magn. Reson. , vol.82 , pp. 309-317
    • Hoffman, B.M.1    Gurbiel, R.J.2
  • 11
    • 48549111357 scopus 로고
    • General theory of polycrystalline ENDOR patterns. G and hyperfine tensors of arbitrary symmetry and relative orientation
    • Hoffman, B. M., J. Martinsen, and R. A. Venters. 1984. General theory of polycrystalline ENDOR patterns. g and hyperfine tensors of arbitrary symmetry and relative orientation. J. Magn. Reson. 59:110-123.
    • (1984) J. Magn. Reson. , vol.59 , pp. 110-123
    • Hoffman, B.M.1    Martinsen, J.2    Venters, R.A.3
  • 12
    • 0001392896 scopus 로고
    • General theory of polycrystalline ENDOR patterns. Effects of finite EPR and ENDOR component linewidths
    • Hoffman, B. M., R. A. Venters, and J. Martinsen. 1985. General theory of polycrystalline ENDOR patterns. Effects of finite EPR and ENDOR component linewidths. J. Magn. Reson. 62:537-542.
    • (1985) J. Magn. Reson. , vol.62 , pp. 537-542
    • Hoffman, B.M.1    Venters, R.A.2    Martinsen, J.3
  • 14
    • 0000389187 scopus 로고
    • Metalloenzyme active-site structure and function through multifrequency CW and pulsed ENDOR
    • L. J. Berliner and J. Reuben, editors. Plenum Press, New York and London.
    • Hoffman, B. M., V. J. DeRose, P. E. Doan, R. J. Gurbiel, A. L. P. Houseman, and J. Telser. 1993. Metalloenzyme active-site structure and function through multifrequency CW and pulsed ENDOR. In Biological Magnetic Resonance, Vol. 13. L. J. Berliner and J. Reuben, editors. Plenum Press, New York and London. 151-218.
    • (1993) Biological Magnetic Resonance , vol.13 , pp. 151-218
    • Hoffman, B.M.1    DeRose, V.J.2    Doan, P.E.3    Gurbiel, R.J.4    Houseman, A.L.P.5    Telser, J.6
  • 17
    • 0019877164 scopus 로고
    • Single crystal EPR of myoglobin nitroxide
    • Hori, H., M. Ikeda-Saito, and I. Yonelani. 1981. Single crystal EPR of myoglobin nitroxide. J. Biol. Chem. 256:7849-7855.
    • (1981) J. Biol. Chem. , vol.256 , pp. 7849-7855
    • Hori, H.1    Ikeda-Saito, M.2    Yonelani, I.3
  • 18
    • 0001176535 scopus 로고
    • Angle-selected ENDOR spectroscopy. 1. Theoretical interpretation of ENDOR shifts from randomly orientated transition-metal complexes
    • Hurst, G. C., T. A. Henderson, and R. W. Kreilick. 1985. Angle-selected ENDOR spectroscopy. 1. Theoretical interpretation of ENDOR shifts from randomly orientated transition-metal complexes. J. Am. Chem. Soc. 107:7294-7299.
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 7294-7299
    • Hurst, G.C.1    Henderson, T.A.2    Kreilick, R.W.3
  • 20
    • 0000261066 scopus 로고
    • ENDOR of randomly oriented mononuclear metalloproteins, Toward structural determinations of the prosthetic group
    • L. J. Berliner and J. Reuben, editors. Plenum Press, New York and London.
    • Huttermann, J. 1993. ENDOR of randomly oriented mononuclear metalloproteins, Toward structural determinations of the prosthetic group. In Biological Magnetic Resonance, Vol. 13. L. J. Berliner and J. Reuben, editors. Plenum Press, New York and London. 219-252.
    • (1993) Biological Magnetic Resonance , vol.13 , pp. 219-252
    • Huttermann, J.1
  • 21
    • 0000779687 scopus 로고
    • Proton ENDOR from randomly oriented NO-ligated haemoglobin: Approaching the structural basis for the R-T transition
    • Huttermann, J., C. Burgard, and R. Kappl. 1994. Proton ENDOR from randomly oriented NO-ligated haemoglobin: approaching the structural basis for the R-T transition. J. Chem. Soc. Faraday Trans. 90: 3077-3087.
    • (1994) J. Chem. Soc. Faraday Trans. , vol.90 , pp. 3077-3087
    • Huttermann, J.1    Burgard, C.2    Kappl, R.3
  • 23
    • 0027949030 scopus 로고
    • The distal residue-CO interaction in carbonmonoxy myoglobins: A molecular dynamics study of two distal histidine tautomers
    • Jewsbury, P., and T. Kitagawa. 1994. The distal residue-CO interaction in carbonmonoxy myoglobins: a molecular dynamics study of two distal histidine tautomers. Biophys. J. 67:2236-2250.
    • (1994) Biophys. J. , vol.67 , pp. 2236-2250
    • Jewsbury, P.1    Kitagawa, T.2
  • 24
    • 85005481091 scopus 로고
    • An ENDOR study of nitrosyl myoglobin single crystals
    • Kappl, R., and J. Hüttermann. 1989. An ENDOR study of nitrosyl myoglobin single crystals. Isr. J. Chem. 29:73-84.
    • (1989) Isr. J. Chem. , vol.29 , pp. 73-84
    • Kappl, R.1    Hüttermann, J.2
  • 25
    • 0003498871 scopus 로고
    • Heme-globin interactions in nitrosylligated hemoglobin as probed by ENDOR spectroscopy
    • A. J. Hoff, editor. Elsevier, Amsterdam.
    • Kappl, R., and J. Hüttermann. 1989. Heme-globin interactions in nitrosylligated hemoglobin as probed by ENDOR spectroscopy. In Advanced EPR: Applications in Biology and Biochemistry. A. J. Hoff, editor. Elsevier, Amsterdam. 501-540.
    • (1989) Advanced Epr: Applications in Biology and Biochemistry , pp. 501-540
    • Kappl, R.1    Hüttermann, J.2
  • 26
    • 0033541085 scopus 로고    scopus 로고
    • 3+ cluster of Ectothiorhodospira halophila iso-II high-potential iron-sulfur protein by ENDOR spectroscopy
    • 3+ cluster of Ectothiorhodospira halophila iso-II high-potential iron-sulfur protein by ENDOR spectroscopy. J. Am. Chem. Soc. 121:1925-1935.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 1925-1935
    • Kappl, R.1    Ciurli, S.2    Luchinat, C.3    Hüttermann, J.4
  • 27
    • 0028328331 scopus 로고
    • Structural determinants of the stretching frequency of CO bound to myoglobin
    • Li, T., M. L. Quillin, G. N. Phillips, Jr., and J. S. Olson. 1994. Structural determinants of the stretching frequency of CO bound to myoglobin. Biochemistry. 33:1433-1446.
    • (1994) Biochemistry. , vol.33 , pp. 1433-1446
    • Li, T.1    Quillin, M.L.2    Phillips G.N., Jr.3    Olson, J.S.4
  • 28
    • 0029647452 scopus 로고
    • Binding of CO to myoglobin from a heme pocket docking site to form nearly linear Fe-C-O
    • Lim, M., T. A. Jackson, and P. A. Anfinrud. 1995. Binding of CO to myoglobin from a heme pocket docking site to form nearly linear Fe-C-O. Science. 269:962-966.
    • (1995) Science , vol.269 , pp. 962-966
    • Lim, M.1    Jackson, T.A.2    Anfinrud, P.A.3
  • 29
    • 0024468312 scopus 로고
    • The effects of E7 and E11 mutations on the kinetics of ligand binding to R-state human hemoglobin
    • Mathews, A. J., R. J. Rohlfs, J. S. Olson, J. Tame, J. P. Renaud, and K. Nagai. 1989. The effects of E7 and E11 mutations on the kinetics of ligand binding to R-state human hemoglobin. J. Biol. Chem. 264: 16573-16583.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16573-16583
    • Mathews, A.J.1    Rohlfs, R.J.2    Olson, J.S.3    Tame, J.4    Renaud, J.P.5    Nagai, K.6
  • 31
    • 0001389357 scopus 로고
    • Electron nuclear double resonance from high-and low-spin ferric hemoglobins and myoglobins
    • Mulks, C. F., C. P. Scholes, L. C. Dickinson, and A. Lapidot. 1979. Electron nuclear double resonance from high-and low-spin ferric hemoglobins and myoglobins. J. Am. Chem. Soc. 101:1645-1654.
    • (1979) J. Am. Chem. Soc. , vol.101 , pp. 1645-1654
    • Mulks, C.F.1    Scholes, C.P.2    Dickinson, L.C.3    Lapidot, A.4
  • 33
    • 0001700962 scopus 로고    scopus 로고
    • Polarization effects on peptide conformations at molecular dynamics simulation
    • Pascutti, P. G., K. C. Mundim, A. S. Ito, and P. M. Bisch. 1999. Polarization effects on peptide conformations at molecular dynamics simulation. J. Comp. Chem. 20:971-982.
    • (1999) J. Comp. Chem. , vol.20 , pp. 971-982
    • Pascutti, P.G.1    Mundim, K.C.2    Ito, A.S.3    Bisch, P.M.4
  • 34
    • 0017301843 scopus 로고
    • Stereochemistry of carbonyl metalloporphyrins - Structure of (pyridine) (carbonyl) (5,10,15,20-tetraphenylporphinato) iron (II)
    • Peng, S. M., and J. A. Ibers. 1976. Stereochemistry of carbonyl metalloporphyrins - structure of (pyridine) (carbonyl) (5,10,15,20-tetraphenylporphinato) iron (II). J. Am. Chem. Soc. 98:8032-8036.
    • (1976) J. Am. Chem. Soc. , vol.98 , pp. 8032-8036
    • Peng, S.M.1    Ibers, J.A.2
  • 35
    • 0014958182 scopus 로고
    • Stereochemistry of cooperative effects in haemoglobin
    • Perutz, M. F. 1970. Stereochemistry of cooperative effects in haemoglobin. Nature. 228:726-734.
    • (1970) Nature , vol.228 , pp. 726-734
    • Perutz, M.F.1
  • 36
    • 0024562782 scopus 로고
    • Myoglobin and hemoglobin - Role of distal residues in reactions with heme ligands
    • Perutz, M. F. 1989. Myoglobin and hemoglobin - role of distal residues in reactions with heme ligands. Trends Biochem. Sci. 14:42-44.
    • (1989) Trends Biochem. Sci. , vol.14 , pp. 42-44
    • Perutz, M.F.1
  • 37
    • 0019209443 scopus 로고
    • Structure and refinement of oxymyoglobin at 1.6 Å resolution
    • Phillips, S. E. V. 1980. Structure and refinement of oxymyoglobin at 1.6 Å resolution. J. Mol. Biol. 142:531-554.
    • (1980) J. Mol. Biol. , vol.142 , pp. 531-554
    • Phillips, S.E.V.1
  • 38
    • 0019827532 scopus 로고
    • Neutron diffraction reveals oxygen-histidine hydrogen bond in oxymyoglobin
    • Phillips, S. E. V., and B. P. Schoenborn. 1981. Neutron diffraction reveals oxygen-histidine hydrogen bond in oxymyoglobin. Nature. 292:81-82.
    • (1981) Nature. , vol.292 , pp. 81-82
    • Phillips, S.E.V.1    Schoenborn, B.P.2
  • 39
    • 0001736551 scopus 로고
    • Kinetic and structural analysis of the effects of pH on carbon monoxide association in myoglobin
    • Quillin, M. L., R. E. Brantley, Jr., K. A. Johnson, and G. Phillips. 1992. Kinetic and structural analysis of the effects of pH on carbon monoxide association in myoglobin. Biophys. J. 61:A466.
    • (1992) Biophys. J. , vol.61
    • Quillin, M.L.1    Brantley R.E., Jr.2    Johnson, K.A.3    Phillips, G.4
  • 40
    • 36849115846 scopus 로고
    • Ligand ENDOR of metal complexes in powders
    • Rist, G. H., and J. S. Hyde. 1970. Ligand ENDOR of metal complexes in powders. J. Chem. Phys. 52:4633-4643.
    • (1970) J. Chem. Phys. , vol.52 , pp. 4633-4643
    • Rist, G.H.1    Hyde, J.S.2
  • 41
    • 0025216601 scopus 로고
    • The effects of amino acid substitution at position E7 (residue 64) on the kinetics of ligand binding to sperm whale myoglobin
    • Rohlfs, R. J., A. J. Mathews, T. E. Carver, J. S. Olson, B. A. Springer, K. D. Egeberg, and S. G. Sligar. 1990. The effects of amino acid substitution at position E7 (residue 64) on the kinetics of ligand binding to sperm whale myoglobin. J. Biol. Chem. 265:3168-3176.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3168-3176
    • Rohlfs, R.J.1    Mathews, A.J.2    Carver, T.E.3    Olson, J.S.4    Springer, B.A.5    Egeberg, K.D.6    Sligar, S.G.7
  • 42
    • 0001428732 scopus 로고
    • Electron nuclear double resonance (ENDOR) from heme and histidine nitrogens in single crystals of aquometmyoglobin
    • Scholes, C. P., A. Lapidot, R. Mascarenhas, T. Inubushi, R. A. Isaacson, and G. Feher. 1982. Electron nuclear double resonance (ENDOR) from heme and histidine nitrogens in single crystals of aquometmyoglobin. J. Am. Chem. Soc. 104:2724-2735.
    • (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
  • 43
    • 0033561577 scopus 로고    scopus 로고
    • EPR and ENDOR studies on CO radicals in γ-irradiated synthetic hydroxyapatites
    • Schramm, D. U., and A. M. Rossi. 1999. EPR and ENDOR studies on CO radicals in γ-irradiated synthetic hydroxyapatites. Phys. Chem. Chem. Phys. 1:2007-2012.
    • (1999) Phys. Chem. Chem. Phys. , vol.1 , pp. 2007-2012
    • Schramm, D.U.1    Rossi, A.M.2
  • 44
    • 0021027685 scopus 로고
    • Structure of human oxyhemoglobin at 2.1 Å resolution
    • Shaanan, B. 1983. Structure of human oxyhemoglobin at 2.1 Å resolution. J. Mol. Biol. 171:31-59.
    • (1983) J. Mol. Biol. , vol.171 , pp. 31-59
    • Shaanan, B.1
  • 45
    • 0024519403 scopus 로고
    • Discrimination between oxygen and carbon monoxide and inhibition of autooxidation by myoglobin site-directed mutagenesis of the distal histidine
    • Springer, B. A., K. D. Egeberg, S. G. Sligar, R. J. Rohlfs, A. J. Mathews, and J. S Olson. 1989. Discrimination between oxygen and carbon monoxide and inhibition of autooxidation by myoglobin site-directed mutagenesis of the distal histidine. J. Biol. Chem. 264:3057-3060.
    • (1989) J. Biol. Chem. , vol.264 , pp. 3057-3060
    • Springer, B.A.1    Egeberg, K.D.2    Sligar, S.G.3    Rohlfs, R.J.4    Mathews, A.J.5    Olson, J.S.6
  • 46
    • 0001818105 scopus 로고
    • Evaluation of hyperfine and quadrupole tensors from ENDOR measurements on single crystals
    • Thuomas, K., and A. Lund. 1975. Evaluation of hyperfine and quadrupole tensors from ENDOR measurements on single crystals. J. Magn. Reson. 18:12-21.
    • (1975) J. Magn. Reson. , vol.18 , pp. 12-21
    • Thuomas, K.1    Lund, A.2
  • 49
    • 0001116126 scopus 로고
    • 57Fe hyperfine coupling tensors of the FeMo cluster in Azotobacter vinelandii MoFe protein: Determination by polycrystalline ENDOR spectroscopy
    • 57Fe hyperfine coupling tensors of the FeMo cluster in Azotobacter vinelandii MoFe protein: determination by polycrystalline ENDOR spectroscopy. J. Am. Chem. Soc. 110: 1935-1943.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 1935-1943
    • True, A.E.1    Nelson, M.J.2    Venters, R.A.3    Orme-Johnson, W.H.4    Hoffman, B.M.5
  • 50
    • 36749114016 scopus 로고
    • EPR study of the structure and spin distribution at the binding site in human nitrosylhemoglobin single crystals
    • Utterback, S. G., D. C. Doetschman, J. Szumowski, and A. K. Rizos. 1983. EPR study of the structure and spin distribution at the binding site in human nitrosylhemoglobin single crystals. J. Chem. Phys. 78: 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
  • 51
    • 0000591302 scopus 로고
    • ENDOR determined molecular geometries of spin-labeled fluoranilides in frozen solution
    • Wells, G. B., and M. W. Makinen. 1988. ENDOR determined molecular geometries of spin-labeled fluoranilides in frozen solution. J. Am. Chem. Soc. 110:6343-6352.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 6343-6352
    • Wells, G.B.1    Makinen, M.W.2


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