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280 related items for PubMed ID: 8639555

  • 1. Three-dimensional structure of the reduced C77S mutant of the Chromatium vinosum high-potential iron-sulfur protein through nuclear magnetic resonance: comparison with the solution structure of the wild-type protein.
    Bentrop D, Bertini I, Capozzi F, Dikiy A, Eltis L, Luchinat C.
    Biochemistry; 1996 May 07; 35(18):5928-36. PubMed ID: 8639555
    [Abstract] [Full Text] [Related]

  • 2. Dynamics of wild-type HiPIPs: a Cys77Ser mutant and a partially unfolded HiPIP.
    Dilg AW, Grantner K, Iakovleva O, Parak FG, Babini E, Bertini I, Capozzi F, Luchinat C, Meyer-Klaucke W.
    J Biol Inorg Chem; 2002 Sep 07; 7(7-8):691-703. PubMed ID: 12203006
    [Abstract] [Full Text] [Related]

  • 3. Detection and classification of hyperfine-shifted 1H, 2H, and 15N resonances of the Rieske ferredoxin component of toluene 4-monooxygenase.
    Xia B, Pikus JD, Xia W, McClay K, Steffan RJ, Chae YK, Westler WM, Markley JL, Fox BG.
    Biochemistry; 1999 Jan 12; 38(2):727-39. PubMed ID: 9888813
    [Abstract] [Full Text] [Related]

  • 4. Three-dimensional solution structure of the oxidized high potential iron-sulfur protein from Chromatium vinosum through NMR. Comparative analysis with the solution structure of the reduced species.
    Bertini I, Dikiy A, Kastrau DH, Luchinat C, Sompornpisut P.
    Biochemistry; 1995 Aug 08; 34(31):9851-8. PubMed ID: 7632685
    [Abstract] [Full Text] [Related]

  • 5. The three-dimensional solution structure of the reduced high-potential iron-sulfur protein from Chromatium vinosum through NMR.
    Banci L, Bertini I, Dikiy A, Kastrau DH, Luchinat C, Sompornpisut P.
    Biochemistry; 1995 Jan 10; 34(1):206-19. PubMed ID: 7819198
    [Abstract] [Full Text] [Related]

  • 6. Use of 1H longitudinal relaxation times in the solution structure of paramagnetic proteins. Application to [4Fe-4S] proteins.
    Huber JG, Moulis JM, Gaillard J.
    Biochemistry; 1996 Oct 01; 35(39):12705-11. PubMed ID: 8841114
    [Abstract] [Full Text] [Related]

  • 7. Factors influencing redox thermodynamics and electron self-exchange for the [Fe4S4] cluster in Chromatium vinosum high potential iron protein: the role of core aromatic residues in defining cluster redox chemistry.
    Soriano A, Li D, Bian S, Agarwal A, Cowan JA.
    Biochemistry; 1996 Sep 24; 35(38):12479-86. PubMed ID: 8823183
    [Abstract] [Full Text] [Related]

  • 8. Comparison and characterization of the [Fe4S4]2+/3+ centre in the wild-type and C77S mutated HiPIPs from Chromatium vinosum monitored by Mössbauer, 57Fe ENDOR and EPR spectroscopies.
    Dilg AW, Capozzi F, Mentler M, Iakovleva O, Luchinat C, Bertini I, Parak FG.
    J Biol Inorg Chem; 2001 Mar 24; 6(3):232-46. PubMed ID: 11315559
    [Abstract] [Full Text] [Related]

  • 9. A complete relaxation matrix refinement of the solution structure of a paramagnetic metalloprotein: reduced HiPIP I from Ectothiorhodospira halophila.
    Bertini I, Felli IC, Luchinat C, Rosato A.
    Proteins; 1996 Feb 24; 24(2):158-64. PubMed ID: 8820483
    [Abstract] [Full Text] [Related]

  • 10. Synthesis, cloning and expression of a synthetic gene for high potential iron protein from Chromatium vinosum.
    Agarwal A, Tan J, Eren M, Tevelev A, Lui SM, Cowan JA.
    Biochem Biophys Res Commun; 1993 Dec 30; 197(3):1357-62. PubMed ID: 7916611
    [Abstract] [Full Text] [Related]

  • 11. Crystal structure and possible dimerization of the high-potential iron-sulfur protein from Chromatium purpuratum.
    Kerfeld CA, Salmeen AE, Yeates TO.
    Biochemistry; 1998 Oct 06; 37(40):13911-7. PubMed ID: 9760225
    [Abstract] [Full Text] [Related]

  • 12. The solution structure refinement of the paramagnetic reduced high-potential iron-sulfur protein I from Ectothiorhodospira halophila by using stable isotope labeling and nuclear relaxation.
    Bertini I, Couture MM, Donaire A, Eltis LD, Felli IC, Luchinat C, Piccioli M, Rosato A.
    Eur J Biochem; 1996 Oct 15; 241(2):440-52. PubMed ID: 8917441
    [Abstract] [Full Text] [Related]

  • 13. Characterization of a partially unfolded high potential iron protein.
    Bertini I, Cowan JA, Luchinat C, Natarajan K, Piccioli M.
    Biochemistry; 1997 Aug 05; 36(31):9332-9. PubMed ID: 9235975
    [Abstract] [Full Text] [Related]

  • 14. Sequential resonance assignments of oxidized high-potential iron-sulfur protein from Chromatium vinosum.
    Nettesheim DG, Harder SR, Feinberg BA, Otvos JD.
    Biochemistry; 1992 Feb 04; 31(4):1234-44. PubMed ID: 1734968
    [Abstract] [Full Text] [Related]

  • 15. Unusual NMR, EPR, and Mössbauer properties of Chromatium vinosum 2[4Fe-4S] ferredoxin.
    Kyritsis P, Kümmerle R, Huber JG, Gaillard J, Guigliarelli B, Popescu C, Münck E, Moulis JM.
    Biochemistry; 1999 May 11; 38(19):6335-45. PubMed ID: 10320364
    [Abstract] [Full Text] [Related]

  • 16. Characterization of an autoreduction pathway for the [Fe4S4]3+ cluster of mutant Chromatium vinosum high-potential iron proteins. Site-directed mutagenesis studies to probe the role of phenylalanine 66 in defining the stability of the [Fe4S4] center provide evidence for oxidative degradation via a [Fe3S4] cluster.
    Bian S, Hemann CF, Hille R, Cowan JA.
    Biochemistry; 1996 Nov 19; 35(46):14544-52. PubMed ID: 8931551
    [Abstract] [Full Text] [Related]

  • 17. Solution structure of the oxidized Fe7S8 ferredoxin from the thermophilic bacterium Bacillus schlegelii by 1H NMR spectroscopy.
    Aono S, Bentrop D, Bertini I, Donaire A, Luchinat C, Niikura Y, Rosato A.
    Biochemistry; 1998 Jul 07; 37(27):9812-26. PubMed ID: 9657695
    [Abstract] [Full Text] [Related]

  • 18. Sequence-specific assignments of the 1H nuclear magnetic resonance spectra of reduced high-potential ferredoxin (HiPIP) from Chromatium vinosum.
    Gaillard J, Albrand JP, Moulis JM, Wemmer DE.
    Biochemistry; 1992 Jun 23; 31(24):5632-9. PubMed ID: 1610810
    [Abstract] [Full Text] [Related]

  • 19. 15N resonance assignments of oxidized and reduced Chromatium vinosum high-potential iron protein.
    Li D, Cottrell CE, Cowan JA.
    J Protein Chem; 1995 Apr 23; 14(3):115-26. PubMed ID: 7576079
    [Abstract] [Full Text] [Related]

  • 20. Solution structure of oxidized rat microsomal cytochrome b5 in the presence of 2 M guanidinium chloride: monitoring the early steps in protein unfolding.
    Arnesano F, Banci L, Bertini I, Koulougliotis D.
    Biochemistry; 1998 Dec 01; 37(48):17082-92. PubMed ID: 9836603
    [Abstract] [Full Text] [Related]

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