메뉴 건너뛰기




Volumn 1384, Issue 1, 1998, Pages 32-42

1H NMR studies of azide binding to cytochrome c

Author keywords

Azide; Cytochrome c; NMR; Two dimensional

Indexed keywords

AZIDE; CYTOCHROME C;

EID: 0032559915     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(97)00210-0     Document Type: Article
Times cited : (9)

References (18)
  • 1
    • 0017927910 scopus 로고
    • Nuclear magnetic resonance studies of hemoproteins: VIII. Proton NMR studies of the binding of various nitrogenous ligands to ferric cytochrome c
    • Morishima I., Ogawa S., Yonezawa T., Iizuka T. Nuclear magnetic resonance studies of hemoproteins: VIII. Proton NMR studies of the binding of various nitrogenous ligands to ferric cytochrome c. Biochim. Biophys. Acta. 532:1978;48-56.
    • (1978) Biochim. Biophys. Acta , vol.532 , pp. 48-56
    • Morishima, I.1    Ogawa, S.2    Yonezawa, T.3    Iizuka, T.4
  • 2
    • 0001263274 scopus 로고
    • Comparative NMR studies of cytochrome c and its active site octapeptide
    • Smith M., Mclendon G. Comparative NMR studies of cytochrome c and its active site octapeptide. J. Am. Chem. Soc. 103:1981;4912-4921.
    • (1981) J. Am. Chem. Soc. , vol.103 , pp. 4912-4921
    • Smith, M.1    Mclendon, G.2
  • 3
  • 4
    • 33748481757 scopus 로고    scopus 로고
    • Nuclear magnetic resonance studies of pyridine binding to cytochrome c
    • G.H. Liu, Y. Chen, W.X. Tang, Nuclear magnetic resonance studies of pyridine binding to cytochrome c, J. Chem. Soc., Dalton Trans. (1997) 795-801.
    • (1997) J. Chem. Soc., Dalton Trans. , pp. 795-801
    • Liu, G.H.1    Chen, Y.2    Tang, W.X.3
  • 6
    • 0028903799 scopus 로고
    • Binding of 1-methylimidazole to cytochrome c: Kinetic analysis and resonance assignments by two-dimensional NMR
    • Shao W.P., Liu G.H., Tang W.X. Binding of 1-methylimidazole to cytochrome c: kinetic analysis and resonance assignments by two-dimensional NMR. Biochim. Biophys. Acta. 1248:1995;177-185.
    • (1995) Biochim. Biophys. Acta , vol.1248 , pp. 177-185
    • Shao, W.P.1    Liu, G.H.2    Tang, W.X.3
  • 7
    • 0029862563 scopus 로고    scopus 로고
    • Structural studies of imidazole-cytochrome c: Resonance assignments and structural comparison with cytochrome c
    • Liu G.H., Shao W.P., Huang X.L., Wu H.M., Tang W.X. Structural studies of imidazole-cytochrome c: resonance assignments and structural comparison with cytochrome c. Biochim. Biophys. Acta. 1277:1996;61-82.
    • (1996) Biochim. Biophys. Acta , vol.1277 , pp. 61-82
    • Liu, G.H.1    Shao, W.P.2    Huang, X.L.3    Wu, H.M.4    Tang, W.X.5
  • 8
    • 33751154791 scopus 로고
    • 1H NMR studies of the imidazole complex of cytochrome c: Resonance assignment and structural characterization of the heme cavity
    • 1H NMR studies of the imidazole complex of cytochrome c: resonance assignment and structural characterization of the heme cavity. Inorg. Chem. 34:1995;680-687.
    • (1995) Inorg. Chem. , vol.34 , pp. 680-687
    • Shao, W.P.1    Sun, H.Z.2    Yao, Y.M.3    Tang, W.X.4
  • 10
    • 84972812731 scopus 로고
    • Application of 2D exchange spectroscopy to the studies of imidazole binding to cytochrome c
    • Shao W.P., Tang W.X. Application of 2D exchange spectroscopy to the studies of imidazole binding to cytochrome c. Spectrosc. Lett. 27:1994;763-773.
    • (1994) Spectrosc. Lett. , vol.27 , pp. 763-773
    • Shao, W.P.1    Tang, W.X.2
  • 12
    • 0023371189 scopus 로고
    • Proton hyperfine resonance assignments using the nuclear overhauser effect for ferric forms of horse and tuna cytochrome c
    • Satterlee J.D., Moench S. Proton hyperfine resonance assignments using the nuclear overhauser effect for ferric forms of horse and tuna cytochrome c. Biophys. J. 52:1987;101-107.
    • (1987) Biophys. J. , vol.52 , pp. 101-107
    • Satterlee, J.D.1    Moench, S.2
  • 13
    • 0022601758 scopus 로고
    • 13C and proton NMR studies of horse cytochrome c, assignment and temperature dependence of methyl resonances
    • 13C and proton NMR studies of horse cytochrome c, assignment and temperature dependence of methyl resonances. FEBS Lett. 194:1986;73-77.
    • (1986) FEBS Lett. , vol.194 , pp. 73-77
    • Santos, H.1    Turner, D.L.2
  • 14
    • 33845281792 scopus 로고
    • 1H NMR studies of the electronic and molecular structure of the heme cavity in horseradish peroxidase, complete heme resonance assignments based on saturation transfer and nuclear overhauser effects
    • 1H NMR studies of the electronic and molecular structure of the heme cavity in horseradish peroxidase, complete heme resonance assignments based on saturation transfer and nuclear overhauser effects. J. Am. Chem. Soc. 109:1987;265-272.
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 265-272
    • Thanabal, V.1    De Ropp, J.S.2    La Mar, G.N.3
  • 15
    • 0025320199 scopus 로고
    • Influence of molecular correlation time on the homonuclear overhauser effect in paramagnetic proteins
    • Dugad L.B., La Mar G.N., Unger S.W. Influence of molecular correlation time on the homonuclear overhauser effect in paramagnetic proteins. J. Am. Chem. Soc. 112:1990;1386-1392.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 1386-1392
    • Dugad, L.B.1    La Mar, G.N.2    Unger, S.W.3
  • 16
    • 0000208839 scopus 로고
    • 5: Assignment of heme propionate resonances on the basis of nuclear overhauser effect measurements and the nature of interprotein contacts with parter redox proteins
    • 5: assignment of heme propionate resonances on the basis of nuclear overhauser effect measurements and the nature of interprotein contacts with parter redox proteins. J. Am. Chem. Soc. 108:1986;1285-1291.
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 1285-1291
    • Mclachlan, S.J.1    La Mar, G.N.2    Sletten, E.3
  • 17
    • 84915716471 scopus 로고
    • Elucidation of cross-relaxation in liquids by two-dimensional NMR spectroscopy
    • Macura S., Ernst R.R. Elucidation of cross-relaxation in liquids by two-dimensional NMR spectroscopy. Mol. Phys. 41:1980;95-107.
    • (1980) Mol. Phys. , vol.41 , pp. 95-107
    • Macura, S.1    Ernst, R.R.2
  • 18
    • 46149139927 scopus 로고
    • Quantitative 2D exchange spectroscopy using time-proportional phase incrementation
    • Johnston E.R., Dellwo M.J., Hendrix J. Quantitative 2D exchange spectroscopy using time-proportional phase incrementation. J. Magn. Reson. 66:1986;399-409.
    • (1986) J. Magn. Reson. , vol.66 , pp. 399-409
    • Johnston, E.R.1    Dellwo, M.J.2    Hendrix, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.