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Journal Abstract Search

116 related items for PubMed ID: 2321966

  • 1. Electrostatic effects on the spectral and redox properties of Clostridium pasteurianum flavodoxin: effects of salt concentration and polylysine.
    Cheddar G, Tollin G.
    Arch Biochem Biophys; 1990 Apr; 278(1):265-8. PubMed ID: 2321966
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  • 2. Kinetics of reduction of high redox potential ferredoxins by the semiquinones of Clostridium pasteurianum flavodoxin and exogenous flavin mononucleotide. Electrostatic and redox potential effects.
    Przysiecki CT, Cheddar G, Meyer TE, Tollin G, Cusanovich MA.
    Biochemistry; 1985 Sep 24; 24(20):5647-52. PubMed ID: 4074719
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  • 4. Kinetic studies of reduction of a 1:1 cytochrome c-flavodoxin complex by free flavin semiquinones and rubredoxin.
    Hazzard JT, Cusanovich MA, Tainer JA, Getzoff ED, Tollin G.
    Biochemistry; 1986 Jun 03; 25(11):3318-28. PubMed ID: 3015203
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  • 5. Transient kinetics of redox reactions of flavodoxin: effects of chemical modification of the flavin mononucleotide prosthetic group on the dynamics of intermediate complex formation and electron transfer.
    Simondsen RP, Tollin G.
    Biochemistry; 1983 Jun 07; 22(12):3008-16. PubMed ID: 6307350
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  • 7. Electron transfer between flavodoxin semiquinone and c-type cytochromes: correlations between electrostatically corrected rate constants, redox potentials, and surface topologies.
    Tollin G, Cheddar G, Watkins JA, Meyer TE, Cusanovich MA.
    Biochemistry; 1984 Dec 18; 23(26):6345-9. PubMed ID: 6099138
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  • 8. Transient kinetics of electron-transfer reactions of flavodoxins.
    Jung J, Tollin G.
    Biochemistry; 1981 Sep 01; 20(18):5124-31. PubMed ID: 7295670
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  • 9. Flavodoxin-cytochrome c interactions: circular dichroism and nuclear magnetic resonance studies.
    Tollin G, Brown K, De Francesco R, Edmondson DE.
    Biochemistry; 1987 Aug 11; 26(16):5042-8. PubMed ID: 2822104
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  • 11. Comparison of electron transfer kinetics between redox proteins free in solution and electrostatically complexed to a lipid bilayer membrane.
    Cheddar G, Tollin G.
    Arch Biochem Biophys; 1994 May 01; 310(2):392-6. PubMed ID: 8179324
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  • 13. Transient kinetics of reduction of blue copper proteins by free flavin and flavodoxin semiquinones.
    Tollin G, Meyer TE, Cheddar G, Getzoff ED, Cusanovich MA.
    Biochemistry; 1986 Jun 03; 25(11):3363-70. PubMed ID: 3730365
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  • 14. Structural and chemical properties of a flavodoxin from Anabaena PCC 7119.
    Fillat MF, Edmondson DE, Gomez-Moreno C.
    Biochim Biophys Acta; 1990 Sep 03; 1040(2):301-7. PubMed ID: 2119231
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  • 15. Role of methionine 56 in the control of the oxidation-reduction potentials of the Clostridium beijerinckii flavodoxin: effects of substitutions by aliphatic amino acids and evidence for a role of sulfur-flavin interactions.
    Druhan LJ, Swenson RP.
    Biochemistry; 1998 Jul 07; 37(27):9668-78. PubMed ID: 9657679
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  • 17. Electrostatic orientation during electron transfer between flavodoxin and cytochrome c.
    Matthew JB, Weber PC, Salemme FR, Richards FM.
    Nature; 1983 Jan 13; 301(5896):169-71. PubMed ID: 6296691
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  • 18. Comparison of the kinetics of reduction and intramolecular electron transfer in electrostatic and covalent complexes of ferredoxin-NADP+ reductase and flavodoxin from Anabaena PCC 7119.
    Walker MC, Pueyo JJ, Gómez-Moreno C, Tollin G.
    Arch Biochem Biophys; 1990 Aug 15; 281(1):76-83. PubMed ID: 2116771
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  • 19. A modified flavodoxin with altered redox potentials is less efficient in electron transfer to nitrogenase.
    Hofstetter W, DerVartanian DV.
    Biochem Biophys Res Commun; 1985 Apr 30; 128(2):643-9. PubMed ID: 3857914
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  • 20. Role of glutamate-59 hydrogen bonded to N(3)H of the flavin mononucleotide cofactor in the modulation of the redox potentials of the Clostridium beijerinckii flavodoxin. Glutamate-59 is not responsible for the pH dependency but contributes to the stabilization of the flavin semiquinone.
    Bradley LH, Swenson RP.
    Biochemistry; 1999 Sep 21; 38(38):12377-86. PubMed ID: 10493805
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