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Journal Abstract Search

133 related items for PubMed ID: 8457586

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  • 2. An investigation of Chromatium vinosum high-potential iron-sulfur protein by EPR and Mossbauer spectroscopy; evidence for a freezing-induced dimerization in NaCl solutions.
    Dunham WR, Hagen WR, Fee JA, Sands RH, Dunbar JB, Humblet C.
    Biochim Biophys Acta; 1991 Sep 20; 1079(3):253-62. PubMed ID: 1655037
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  • 3. Investigation of the role of a surface patch in the self-association of Chromatium vinosum high potential iron-sulfur protein.
    Couture MM, Auger M, Rosell F, Mauk AG, Boubour E, Lennox RB, Eltis LD.
    Biochim Biophys Acta; 1999 Aug 17; 1433(1-2):159-69. PubMed ID: 10446369
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  • 4. 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
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  • 9. 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
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  • 13. Elucidation of a [4Fe-4S] cluster degradation pathway: rapid kinetic studies of the degradation of Chromatium vinosum HiPIP.
    Foster MW, Bian S, Surerus KK, Cowan JA.
    J Biol Inorg Chem; 2001 Mar 07; 6(3):266-74. PubMed ID: 11315562
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  • 16. 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
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  • 17. Primary structure of Chromatium tepidum high-potential iron-sulfur protein in relation to thermal denaturation.
    Moulis JM, Scherrer N, Gagnon J, Forest E, Petillot Y, Garcia D.
    Arch Biochem Biophys; 1993 Aug 15; 305(1):186-92. PubMed ID: 8393645
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  • 18. Steady-state and time-resolved fluorescence studies on wild type and mutant chromatium vinosum high potential iron proteins: holo- and apo-forms.
    Sau AK, Chen CA, Cowan JA, Mazumdar S, Mitra S.
    Biophys J; 2001 Oct 15; 81(4):2320-30. PubMed ID: 11566801
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  • 19. The molecular structure of the high potential iron-sulfur protein isolated from Ectothiorhodospira halophila determined at 2.5-A resolution.
    Breiter DR, Meyer TE, Rayment I, Holden HM.
    J Biol Chem; 1991 Oct 05; 266(28):18660-7. PubMed ID: 1917989
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