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Journal Abstract Search

240 related items for PubMed ID: 10572002

  • 1. Enhanced efficiency of ATP hydrolysis during nitrogenase catalysis utilizing reductants that form the all-ferrous redox state of the Fe protein.
    Erickson JA, Nyborg AC, Johnson JL, Truscott SM, Gunn A, Nordmeyer FR, Watt GD.
    Biochemistry; 1999 Oct 26; 38(43):14279-85. PubMed ID: 10572002
    [Abstract] [Full Text] [Related]

  • 2. Evidence for a two-electron transfer using the all-ferrous Fe protein during nitrogenase catalysis.
    Nyborg AC, Johnson JL, Gunn A, Watt GD.
    J Biol Chem; 2000 Dec 15; 275(50):39307-12. PubMed ID: 11005818
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  • 3. Evidence for electron transfer from the nitrogenase iron protein to the molybdenum-iron protein without MgATP hydrolysis: characterization of a tight protein-protein complex.
    Lanzilotta WN, Fisher K, Seefeldt LC.
    Biochemistry; 1996 Jun 04; 35(22):7188-96. PubMed ID: 8679547
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  • 4. Nitrogenase of Azotobacter vinelandii: kinetic analysis of the Fe protein redox cycle.
    Duyvis MG, Wassink H, Haaker H.
    Biochemistry; 1998 Dec 15; 37(50):17345-54. PubMed ID: 9860849
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  • 5. Effects on substrate reduction of substitution of histidine-195 by glutamine in the alpha-subunit of the MoFe protein of Azotobacter vinelandii nitrogenase.
    Dilworth MJ, Fisher K, Kim CH, Newton WE.
    Biochemistry; 1998 Dec 15; 37(50):17495-505. PubMed ID: 9860864
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  • 6. Nucleotide-assisted [Fe4S4] redox state interconversions of the Azotobacter vinelandii Fe protein and their relevance to nitrogenase catalysis.
    Jacobs D, Watt GD.
    Biochemistry; 2013 Jul 16; 52(28):4791-9. PubMed ID: 23815521
    [Abstract] [Full Text] [Related]

  • 7. Evidence That the Pi Release Event Is the Rate-Limiting Step in the Nitrogenase Catalytic Cycle.
    Yang ZY, Ledbetter R, Shaw S, Pence N, Tokmina-Lukaszewska M, Eilers B, Guo Q, Pokhrel N, Cash VL, Dean DR, Antony E, Bothner B, Peters JW, Seefeldt LC.
    Biochemistry; 2016 Jul 05; 55(26):3625-35. PubMed ID: 27295169
    [Abstract] [Full Text] [Related]

  • 8. Pre-steady-state MgATP-dependent proton production and electron transfer by nitrogenase from Azotobacter vinelandii.
    Duyvis MG, Wassink H, Haaker H.
    Eur J Biochem; 1994 Nov 01; 225(3):881-90. PubMed ID: 7957225
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  • 9. Hydrolysis of nucleoside triphosphates other than ATP by nitrogenase.
    Ryle MJ, Seefeldt LC.
    J Biol Chem; 2000 Mar 03; 275(9):6214-9. PubMed ID: 10692415
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  • 10. The role of MgATP hydrolysis in nitrogenase catalysis.
    Cordewener J, Krüse-Wolters M, Wassink H, Haaker H, Veeger C.
    Eur J Biochem; 1988 Mar 15; 172(3):739-45. PubMed ID: 2965012
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  • 11. Reactions of Azotobacter vinelandii nitrogenase using Ti(III) as reductant.
    Nyborg AC, Erickson JA, Johnson JL, Gunn A, Truscott SM, Watt GD.
    J Inorg Biochem; 2000 Mar 15; 78(4):371-81. PubMed ID: 10857919
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  • 17. Formation of a tight 1:1 complex of Clostridium pasteurianum Fe protein-Azotobacter vinelandii MoFe protein: evidence for long-range interactions between the Fe protein binding sites during catalytic hydrogen evolution.
    Clarke TA, Maritano S, Eady RR.
    Biochemistry; 2000 Sep 19; 39(37):11434-40. PubMed ID: 10985789
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  • 20. Pre-steady-state kinetics of nitrogenase from Azotobacter vinelandii. Evidence for an ATP-induced conformational change of the nitrogenase complex as part of the reaction mechanism.
    Duyvis MG, Wassink H, Haaker H.
    J Biol Chem; 1996 Nov 22; 271(47):29632-6. PubMed ID: 8939894
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