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109 related items for PubMed ID: 8931551

  • 1. 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
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  • 2. 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
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  • 3. Role of aromatic residues in stabilization of the [Fe4S4] cluster in high-potential iron proteins (HiPIPs): physical characterization and stability studies of Tyr-19 mutants of Chromatium vinosum HiPIP.
    Agarwal A, Li D, Cowan JA.
    Proc Natl Acad Sci U S A; 1995 Oct 10; 92(21):9440-4. PubMed ID: 7568150
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  • 4. Electron transfer from HiPIP to the photooxidized tetraheme cytochrome subunit of Allochromatium vinosum reaction center: new insights from site-directed mutagenesis and computational studies.
    Venturoli G, Mamedov MD, Mansy SS, Musiani F, Strocchi M, Francia F, Semenov AY, Cowan JA, Ciurli S.
    Biochemistry; 2004 Jan 20; 43(2):437-45. PubMed ID: 14717598
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  • 5. 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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  • 6. 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
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  • 7. The role of a conserved tyrosine residue in high-potential iron sulfur proteins.
    Iwagami SG, Creagh AL, Haynes CA, Borsari M, Felli IC, Piccioli M, Eltis LD.
    Protein Sci; 1995 Dec 05; 4(12):2562-72. PubMed ID: 8580847
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  • 8. 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
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  • 9. Role of the [4Fe-4S] cluster in reductive activation of the cobalt center of the corrinoid iron-sulfur protein from Clostridium thermoaceticum during acetate biosynthesis.
    Menon S, Ragsdale SW.
    Biochemistry; 1998 Apr 21; 37(16):5689-98. PubMed ID: 9548955
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  • 11. Structural and dynamical properties of a partially unfolded Fe4S4 protein: role of the cofactor in protein folding.
    Bentrop D, Bertini I, Iacoviello R, Luchinat C, Niikura Y, Piccioli M, Presenti C, Rosato A.
    Biochemistry; 1999 Apr 13; 38(15):4669-80. PubMed ID: 10200154
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  • 13. [Evaluation of effect of the peptide structure on energetics of reduction-oxidation reactions of proteins containing Fe4S4 clusters in computer experiments].
    Ivaĭkina AG, Balabaev NK, Shaĭtan KV.
    Biofizika; 2001 Apr 13; 46(4):589-94. PubMed ID: 11558366
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  • 14. 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 13; 7(7-8):691-703. PubMed ID: 12203006
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  • 15. 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 13; 6(3):232-46. PubMed ID: 11315559
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  • 16. 15N resonance assignments of oxidized and reduced Chromatium vinosum high-potential iron protein.
    Li D, Cottrell CE, Cowan JA.
    J Protein Chem; 1995 Apr 13; 14(3):115-26. PubMed ID: 7576079
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  • 17. The IscA from Acidithiobacillus ferrooxidans is an iron-sulfur protein which assemble the [Fe4S4] cluster with intracellular iron and sulfur.
    Zeng J, Geng M, Jiang H, Liu Y, Liu J, Qiu G.
    Arch Biochem Biophys; 2007 Jul 15; 463(2):237-44. PubMed ID: 17470358
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