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Volumn 267, Issue 1, 2000, Pages 216-221

Assignment of heme methyl 1H-NMR resonances of high-spin and low-spin ferric complexes of cytochrome P450cam using one-dimensional and two- dimensional paramagnetic signals enhancement (PASE) magnetization transfer experiments

Author keywords

Cytochrome P450; Isocyanides; NMR; Paramagnetic

Indexed keywords

CAMPHOR; CYANIDE; CYTOCHROME P450; HEME; IRON COMPLEX;

EID: 0012001112     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2000.00995.x     Document Type: Article
Times cited : (10)

References (25)
  • 3
    • 33845281095 scopus 로고
    • Cytochrome P-450 and chloroperoxidase: Thiolate-ligated heme enzymes. Spectroscopic determination of their active site structures and mechanistic implications of thiolate ligation
    • 3. Dawson, J.H. & Sono, M. (1987) Cytochrome P-450 and chloroperoxidase: thiolate-ligated heme enzymes. spectroscopic determination of their active site structures and mechanistic implications of thiolate ligation. Chem. Rev. 87, 1255-1276.
    • (1987) Chem. Rev. , vol.87 , pp. 1255-1276
    • Dawson, J.H.1    Sono, M.2
  • 4
    • 0028970162 scopus 로고
    • Substrate interactions in Cytochrome P450: Correlation between carbon-13 nuclear magnetic resonance chemical shifts and C-O vibrational frequencies
    • 4. Legrand, N., Bondon, A., Simonneaux, G., Jung, C. & Gill, E. (1995) Substrate interactions in Cytochrome P450: correlation between carbon-13 nuclear magnetic resonance chemical shifts and C-O vibrational frequencies. FEBS Lett. 364, 152-156.
    • (1995) FEBS Lett. , vol.364 , pp. 152-156
    • Legrand, N.1    Bondon, A.2    Simonneaux, G.3    Jung, C.4    Gill, E.5
  • 5
    • 0031559605 scopus 로고    scopus 로고
    • 1H-NMR study of diamagnetic cytochrome P450cam: Assignment of heme resonances and subtrate dependance of one cysteinate β proton
    • 5. Mouro, C., Bondon, A., Simonneaux, G. & Jung, C. (1997) 1H-NMR study of diamagnetic cytochrome P450cam: assignment of heme resonances and subtrate dependance of one cysteinate β proton. FEBS Lett. 414, 203-208.
    • (1997) FEBS Lett. , vol.414 , pp. 203-208
    • Mouro, C.1    Bondon, A.2    Simonneaux, G.3    Jung, C.4
  • 6
    • 0015385888 scopus 로고
    • Proton magnetic resonance reveals high-spin iron (II) in ferrous cytochrome P450cam from Pseudomonas putida
    • 6. Keller, R.M., Wüthrich, K. & Debrunner, P. (1972) Proton magnetic resonance reveals high-spin iron (II) in ferrous cytochrome P450cam from Pseudomonas putida. Proc. Natl Acad. Sci. USA 69, 2073-2075.
    • (1972) Proc. Natl Acad. Sci. USA , vol.69 , pp. 2073-2075
    • Keller, R.M.1    Wüthrich, K.2    Debrunner, P.3
  • 7
    • 0004140036 scopus 로고
    • Cytochrome P450
    • Academic Press, New York
    • 7. Sato, O. & Omura, T. (1978). In Cytochrome P450, pp. 127-131. Academic Press, New York.
    • (1978) , pp. 127-131
    • Sato, O.1    Omura, T.2
  • 9
    • 0025064065 scopus 로고
    • A nuclear magnetic resonance study of axial ligation for the reduced states of chloroperoxidase, cytochrome P-450cam and porphyrinatoiron (II) thiolate complexes
    • 9. Lukat, G.S. & Goff, H.M. (1990) A nuclear magnetic resonance study of axial ligation for the reduced states of chloroperoxidase, cytochrome P-450cam and porphyrinatoiron (II) thiolate complexes. Biochim. Biophys. Acta 1037, 351-359.
    • (1990) Biochim. Biophys. Acta , vol.1037 , pp. 351-359
    • Lukat, G.S.1    Goff, H.M.2
  • 10
    • 0027217930 scopus 로고
    • Spectroscopic characterization of a newly isolated cytochrome P450 from Rhodococcus rhodochrous
    • 10. Banci, L., Bertini, I., Eltis, L.D. & Pieratelli, R. (1993) Spectroscopic characterization of a newly isolated cytochrome P450 from Rhodococcus rhodochrous. Biophys. J. 65, 806-813.
    • (1993) Biophys. J. , vol.65 , pp. 806-813
    • Banci, L.1    Bertini, I.2    Eltis, L.D.3    Pieratelli, R.4
  • 11
    • 0027337099 scopus 로고
    • 1H-NMR study of reduced heme proteins myoglobin and cytochrome P450
    • 11. Banci, L., Bertini, I., Marconi, S. & Pierattelli, R. (1993) 1H-NMR study of reduced heme proteins myoglobin and cytochrome P450. Eur. J. Biochem. 215, 431-437.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 431-437
    • Banci, L.1    Bertini, I.2    Marconi, S.3    Pierattelli, R.4
  • 13
    • 0030444041 scopus 로고    scopus 로고
    • NMR studies of recombinant cytochrome P450cam mutants
    • 13. Wakasugi, K., Ishimori, K. & Morishima, I. (1996) NMR studies of recombinant cytochrome P450cam mutants. Biochimie 78, 763-770.
    • (1996) Biochimie , vol.78 , pp. 763-770
    • Wakasugi, K.1    Ishimori, K.2    Morishima, I.3
  • 14
    • 0018801486 scopus 로고
    • The effect of cytochrome P-450cam on the NMR relaxation rate of water protons
    • 14. Philson, S.B., Debruner, P.G., Schmidt, P.G. & Gunsalus, I.C. (1979) The effect of cytochrome P-450cam on the NMR relaxation rate of water protons. J. Biol. Chem. 254, 10173-10179.
    • (1979) J. Biol. Chem. , vol.254 , pp. 10173-10179
    • Philson, S.B.1    Debruner, P.G.2    Schmidt, P.G.3    Gunsalus, I.C.4
  • 15
    • 0032807659 scopus 로고    scopus 로고
    • Proton nuclear magnetic resonance study of the binary complex of cytochrome P450cam and putidaredoxin: Interaction and electron transfer rate analysis
    • 15. Mouro, C., Bondon, A., Jung, C., de Certaines, J.D., Spencer, R.G.S. & Simonneaux, G. (1999) Proton nuclear magnetic resonance study of the binary complex of cytochrome P450cam and putidaredoxin: interaction and electron transfer rate analysis. FEBS Lett. 455, 302-306.
    • (1999) FEBS Lett. , vol.455 , pp. 302-306
    • Mouro, C.1    Bondon, A.2    Jung, C.3    De Certaines, J.D.4    Spencer, R.G.S.5    Simonneaux, G.6
  • 16
    • 0032162089 scopus 로고    scopus 로고
    • PASE (PAramagnetic Signals Enhancement): A new method for NMR study of paramagnetic proteins
    • 16. Bondon, A. & Mouro, C. (1998) PASE (PAramagnetic Signals Enhancement): a new method for NMR study of paramagnetic proteins. J. Magn. Res. 134, 154-157.
    • (1998) J. Magn. Res. , vol.134 , pp. 154-157
    • Bondon, A.1    Mouro, C.2
  • 17
    • 0027096449 scopus 로고
    • Substrate analogue induced changes of the CO-stretching mode multiplicity in cytochrome P-450cam carbon monoxide complex
    • 17. Jung, C., Hui Bon Hoa, G., Schröder, K.-L., Simon, M. & Doucet, J.P. (1992) Substrate analogue induced changes of the CO-stretching mode multiplicity in cytochrome P-450cam carbon monoxide complex. Biochemistry 35, 12855-12862.
    • (1992) Biochemistry , vol.35 , pp. 12855-12862
    • Jung, C.1    Hui Bon Hoa, G.2    Schröder, K.-L.3    Simon, M.4    Doucet, J.P.5
  • 18
    • 0024974060 scopus 로고
    • Crystal structure of the carbon monoxide-substrate-cytochrome P-450cam ternary complex
    • 18. Raag, R. & Poulos, T.L. (1989) Crystal structure of the carbon monoxide-substrate-cytochrome P-450cam ternary complex. Biochemistry 28, 7586-7592.
    • (1989) Biochemistry , vol.28 , pp. 7586-7592
    • Raag, R.1    Poulos, T.L.2
  • 19
    • 0015087968 scopus 로고
    • Ethyl isocyanide complexes of bacterial cytochrome P-450
    • 19. Griffin, B. & Peterson, J.A. (1971) Ethyl isocyanide complexes of bacterial cytochrome P-450. Arch. Biochem. Biophys. 145, 220-229.
    • (1971) Arch. Biochem. Biophys. , vol.145 , pp. 220-229
    • Griffin, B.1    Peterson, J.A.2
  • 20
    • 0029806798 scopus 로고    scopus 로고
    • Structural changes in cytochrome P-450cam effected by the binding of the enantiomers (1R-camphor and (1S)-camphor
    • 20. Schulze, H., Hui Bon Hoa, G., Helms, V., Wade, R.C. & Jung, C. (1996) Structural changes in cytochrome P-450cam effected by the binding of the enantiomers (1R)-camphor and (1S)-camphor. Biochemistry 35, 14127-14138.
    • (1996) Biochemistry , vol.35 , pp. 14127-14138
    • Schulze, H.1    Hui Bon Hoa, G.2    Helms, V.3    Wade, R.C.4    Jung, C.5
  • 21
    • 0023055752 scopus 로고
    • NMR study of the molecular and electronic structure of the heme cavity of Aplysia metmyoglobin. Resonance assignments based on isotope labeling and proton nuclear Overhauser effect measurements
    • 21. Pande, U., La Mar, G.N., Lecomte, J.T.J., Ascoli, F., Brunori, M., Smith, K.M., Pandey, R.K., Parish, D.W. & Thanabal, V. (1986) NMR study of the molecular and electronic structure of the heme cavity of Aplysia metmyoglobin. Resonance assignments based on isotope labeling and proton nuclear Overhauser effect measurements. Biochemistry 25, 5638-5646.
    • (1986) Biochemistry , vol.25 , pp. 5638-5646
    • Pande, U.1    La Mar, G.N.2    Lecomte, J.T.J.3    Ascoli, F.4    Brunori, M.5    Smith, K.M.6    Pandey, R.K.7    Parish, D.W.8    Thanabal, V.9
  • 22
    • 0019223598 scopus 로고
    • Equilibrium binding of alkyl isocyanides to human hemoglobin
    • 22. Reisberg, P.I. & Olson, J.S. (1980) Equilibrium binding of alkyl isocyanides to human hemoglobin. J. Biol. Chem. 255, 4144-4150.
    • (1980) J. Biol. Chem. , vol.255 , pp. 4144-4150
    • Reisberg, P.I.1    Olson, J.S.2
  • 23
    • 33845281792 scopus 로고
    • 1H NMR study of the electronic and molecular structure of the heme cavity in horseradish peroxidase. Complete heme resonance assignment based on saturation transfer and nuclear Overhauser effects
    • 23. Thanabal, V., de Ropp, J.S. & La Mar, G.N. (1987) 1H NMR study of the electronic and molecular structure of the heme cavity in horseradish peroxidase. Complete heme resonance assignment based on saturation transfer and nuclear Overhauser effects. J. Am. Chem. Soc. 109, 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
  • 24
    • 0001215890 scopus 로고
    • Nuclear magnetic resonance of paramagnetic metalloproteins
    • 24. Bertini, I., Turano, P. & Vila, A.J. (1993) Nuclear magnetic resonance of paramagnetic metalloproteins. Chem. Rev. 93, 2833-2932.
    • (1993) Chem. Rev. , vol.93 , pp. 2833-2932
    • Bertini, I.1    Turano, P.2    Vila, A.J.3
  • 25
    • 0026518909 scopus 로고
    • Proton nuclear Overhauser effect study of the heme active site structure of chloroperoxidase
    • 25. Dugad, L.B., Wang, X., Wang, C.-C., Lukat, G.S. & Goff, H.M. (1992) Proton nuclear Overhauser effect study of the heme active site structure of chloroperoxidase. Biochemistry 31, 1651-1655.
    • (1992) Biochemistry , vol.31 , pp. 1651-1655
    • Dugad, L.B.1    Wang, X.2    Wang, C.-C.3    Lukat, G.S.4    Goff, H.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.