메뉴 건너뛰기




Volumn 24, Issue 2, 1996, Pages 158-164

A complete relaxation matrix refinement of the solution structure of a paramagnetic metalloprotein: Reduced HiPIP I from Ectothiorhodospira halophila

Author keywords

iron sulfur proteins; NMR; nuclear Overhauser effect; paramagnetic relaxation; relaxation matrix analysis

Indexed keywords

BACTERIAL PROTEIN; IRON SULFUR PROTEIN; METALLOPROTEIN;

EID: 0029865939     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199602)24:2<158::AID-PROT3>3.0.CO;2-F     Document Type: Article
Times cited : (27)

References (26)
  • 1
    • 0028004661 scopus 로고
    • The three dimensional structure in solution of the paramagnetic protein HiPIP I from Ectothiorhodospira halophila through nuclear magnetic resonance
    • Banci, L., Bertini, L, Eltis, L.D., Felli, I.C., Kastrau, D.H.W., Luchinat, C., Piccioli, M., Pierattelli, R., Smith, M. The three dimensional structure in solution of the paramagnetic protein HiPIP I from Ectothiorhodospira halophila through nuclear magnetic resonance. Eur. J. Biochem. 225:715-725, 1994.
    • (1994) Eur. J. Biochem. , vol.225 , pp. 715-725
    • Banci, L.1    Bertini, L.2    Eltis, L.D.3    Felli, I.C.4    Kastrau, D.H.W.5    Luchinat, C.6    Piccioli, M.7    Pierattelli, R.8    Smith, M.9
  • 2
    • 0028908669 scopus 로고
    • The tridimensional solution structure of the reduced high potential iron sulfur protein from Chromatium vinosum through NMR
    • Banci, L., Bertini, I., Dikiy, A., Kastrau, D.H.W., Luchinat, C., Sompornpisut, P. The tridimensional solution structure of the reduced high potential iron sulfur protein from Chromatium vinosum through NMR. Biochemistry 34:206-219, 1995.
    • (1995) Biochemistry , vol.34 , pp. 206-219
    • Banci, L.1    Bertini, I.2    Dikiy, A.3    Kastrau, D.H.W.4    Luchinat, C.5    Sompornpisut, P.6
  • 3
    • 0029126461 scopus 로고
    • The three dimensional solution structure of the oxidized HiPIP from Chromatium vinosum through NMR. Comparative analysis with the solution structure of the reduced species
    • Bertini, I., Dikiy, A., Kastrau, D.H.W., Luchinat, C., Sompornpisut, P. The three dimensional solution structure of the oxidized HiPIP from Chromatium vinosum through NMR. Comparative analysis with the solution structure of the reduced species. Biochemistry 34:9851-9858, 1995.
    • (1995) Biochemistry , vol.34 , pp. 9851-9858
    • Bertini, I.1    Dikiy, A.2    Kastrau, D.H.W.3    Luchinat, C.4    Sompornpisut, P.5
  • 4
    • 0029115741 scopus 로고
    • The three dimensional solution structure of the cyanide adduct of Saccharomyces cerevisiae Met80Ala-iso-1-cytochrome c. Identification of ligand-residue interactions in the distal heme cavity
    • Banci, L., Bertini, I., Bren, K.L., Gray, H.B., Sompornpisut, P., Turano, P. The three dimensional solution structure of the cyanide adduct of Saccharomyces cerevisiae Met80Ala-iso-1-cytochrome c. Identification of ligand-residue interactions in the distal heme cavity. Biochemistry 34:11385-11398, 1995.
    • (1995) Biochemistry , vol.34 , pp. 11385-11398
    • Banci, L.1    Bertini, I.2    Bren, K.L.3    Gray, H.B.4    Sompornpisut, P.5    Turano, P.6
  • 5
    • 9044220258 scopus 로고
    • The solution structure of oxidized HiPIP I from Ectothiorhodospira halophila. Can NMR probe rearrangements be associated to electron transfer processes?
    • in press
    • Bertini, I., Eltis, L.D., Felli, I.C., Kastrau, D.H.W., Luchinat, C., Piccioli, M. The solution structure of oxidized HiPIP I from Ectothiorhodospira halophila. Can NMR probe rearrangements be associated to electron transfer processes? Chemistry 1995 (in press).
    • (1995) Chemistry
    • Bertini, I.1    Eltis, L.D.2    Felli, I.C.3    Kastrau, D.H.W.4    Luchinat, C.5    Piccioli, M.6
  • 8
    • 0028307538 scopus 로고
    • An NMR-derived model for the solution structure of oxidized putidaredoxin, a 2-Fe, 2-S ferredoxin from Pseudomonas
    • Pochapsky, T.C., Mei Ye, X., Ratnaswamy, G., Lyons, T.A. An NMR-derived model for the solution structure of oxidized putidaredoxin, a 2-Fe, 2-S ferredoxin from Pseudomonas. Biochemistry 33:6424-6432, 1994.
    • (1994) Biochemistry , vol.33 , pp. 6424-6432
    • Pochapsky, T.C.1    Mei Ye, X.2    Ratnaswamy, G.3    Lyons, T.A.4
  • 9
    • 0039421618 scopus 로고
    • The development of nuclear magnetic resonance spectroscopy as a technique for protein structure determination
    • Wüthrich, K. The development of nuclear magnetic resonance spectroscopy as a technique for protein structure determination. Ace. Chem. Res. 22:36-44, 1989.
    • (1989) Ace. Chem. Res. , vol.22 , pp. 36-44
    • Wüthrich, K.1
  • 10
    • 0001758043 scopus 로고
    • Iterative procedure for structure determination from proton-proton NOEs using a full relaxation matrix approach. Application to a DNA octamer
    • Boelens, R., Koning, T.M.G., Van der Marel, G.A., Van Boom, J.H., Kaptein, R. Iterative procedure for structure determination from proton-proton NOEs using a full relaxation matrix approach. Application to a DNA octamer. J. Magn. Reson. 82:290-308, 1989.
    • (1989) J. Magn. Reson. , vol.82 , pp. 290-308
    • Boelens, R.1    Koning, T.M.G.2    Van Der Marel, G.A.3    Van Boom, J.H.4    Kaptein, R.5
  • 11
    • 0026340030 scopus 로고
    • The solution structure of mohtin from NMR distance constraints, distance geometry, molecular dynamics, and an iterative full relaxation matrix refinement
    • Edmondson, S., Khan, N., Shriver, J., Zdunek, J., Gräslund, A. The solution structure of mohtin from NMR distance constraints, distance geometry, molecular dynamics, and an iterative full relaxation matrix refinement. Biochemistry 30:11271-11279, 1991.
    • (1991) Biochemistry , vol.30 , pp. 11271-11279
    • Edmondson, S.1    Khan, N.2    Shriver, J.3    Zdunek, J.4    Gräslund, A.5
  • 12
    • 0001053688 scopus 로고
    • A theoretical study of distance determinations from NMR. Two-dimensional nuclear Overhauser effect spectra
    • Keepers, J.W., James, T.L. A theoretical study of distance determinations from NMR. Two-dimensional nuclear Overhauser effect spectra. J. Magn. Reson. 57:404-426, 1984.
    • (1984) J. Magn. Reson. , vol.57 , pp. 404-426
    • Keepers, J.W.1    James, T.L.2
  • 14
    • 0002250750 scopus 로고
    • A simple method for the refinement of models derived from NMR data demonstrated on a zinc-finger domain from yeast ADR1
    • Hoffmann, R.C., Xu, R.X., Klevit, R.E., Herriott, J.R. A simple method for the refinement of models derived from NMR data demonstrated on a zinc-finger domain from yeast ADR1. J. Magn. Reson. [B] 102:61-72, 1993.
    • (1993) J. Magn. Reson. [B] , vol.102 , pp. 61-72
    • Hoffmann, R.C.1    Xu, R.X.2    Klevit, R.E.3    Herriott, J.R.4
  • 16
    • 0018977856 scopus 로고
    • Interpretation of the Mossbauer spectra of the high-potential iron protein from chromatium
    • Middleton, P., Dickson, D.P.E., Johnson, C.E., Rush, J.D. Interpretation of the Mossbauer spectra of the high-potential iron protein from chromatium. Eur. J. Biochem. 104: 289-296, 1980.
    • (1980) Eur. J. Biochem. , vol.104 , pp. 289-296
    • Middleton, P.1    Dickson, D.P.E.2    Johnson, C.E.3    Rush, J.D.4
  • 17
    • 0028171933 scopus 로고
    • 15N nuclear magnetic resonance spectra of the reduced recombinant high potential iron sulfur protein (HiPIP) I from Ectothiorhodospira halophila
    • 15N nuclear magnetic resonance spectra of the reduced recombinant high potential iron sulfur protein (HiPIP) I from Ectothiorhodospira halophila. Eur. J. Biochem. 225:703-714, 1994.
    • (1994) Eur. J. Biochem. , vol.225 , pp. 703-714
    • Bertini, I.1    Felli, I.C.2    Kastrau, D.H.W.3    Luchinat, C.4    Piccioli, M.5    Viezzoli, M.S.6
  • 19
    • 0026089657 scopus 로고
    • Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA
    • Güntert, P., Braun, W., Wüthrich, K. Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA. J. Mol. Biol. 217:517-530, 1991.
    • (1991) J. Mol. Biol. , vol.217 , pp. 517-530
    • Güntert, P.1    Braun, W.2    Wüthrich, K.3
  • 20
    • 0026259488 scopus 로고
    • Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints
    • Güntert, P., Wüthrich, K. Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints. J. Biomol. NMR 1:447-456, 1991.
    • (1991) J. Biomol. NMR , vol.1 , pp. 447-456
    • Güntert, P.1    Wüthrich, K.2
  • 21
    • 0002711832 scopus 로고
    • Nuclear relaxation in macromolecules by paramagnetic ions: A novel mechanism
    • Guéron, M Nuclear relaxation in macromolecules by paramagnetic ions: A novel mechanism. J. Magn. Reson. 19:58-66, 1975.
    • (1975) J. Magn. Reson. , vol.19 , pp. 58-66
    • Guéron, M.1
  • 22
    • 0000524487 scopus 로고
    • Nuclear relaxation processes of paramagnetic complexes. the slow motion case
    • Vega, A.J., Fiat, D. Nuclear relaxation processes of paramagnetic complexes. The slow motion case. Mol. Phys. 31: 347-362, 1976.
    • (1976) Mol. Phys. , vol.31 , pp. 347-362
    • Vega, A.J.1    Fiat, D.2
  • 23
    • 36849133491 scopus 로고
    • Nuclear magnetic interactions in the HF molecule
    • Solomon, I., Bloembergen, N. Nuclear magnetic interactions in the HF molecule. J. Chem. Phys. 25:261-266, 1956.
    • (1956) J. Chem. Phys. , vol.25 , pp. 261-266
    • Solomon, I.1    Bloembergen, N.2
  • 24
    • 36849117843 scopus 로고
    • Proton relaxation times in paramagnetic solutions
    • Bloembergen, N. Proton relaxation times in paramagnetic solutions. J. Chem. Phys. 27:572-573, 1957.
    • (1957) J. Chem. Phys. , vol.27 , pp. 572-573
    • Bloembergen, N.1
  • 25
    • 36149008265 scopus 로고
    • Relaxation processes in a system of two spins
    • Solomon, I. Relaxation processes in a system of two spins. Phys. Rev. 99:559-565, 1955.
    • (1955) Phys. Rev. , vol.99 , pp. 559-565
    • Solomon, I.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.