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190 related items for PubMed ID: 1656943

  • 1. Klebsiella pneumoniae nitrogenase. The pre-steady-state kinetics of MoFe-protein reduction and hydrogen evolution under conditions of limiting electron flux show that the rates of association with the Fe-protein and electron transfer are independent of the oxidation level of the MoFe-protein.
    Fisher K, Lowe DJ, Thorneley RN.
    Biochem J; 1991 Oct 01; 279 ( Pt 1)(Pt 1):81-5. PubMed ID: 1656943
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  • 2. The mechanism of Klebsiella pneumoniae nitrogenase action. Pre-steady-state kinetics of H2 formation.
    Lowe DJ, Thorneley RN.
    Biochem J; 1984 Dec 15; 224(3):877-86. PubMed ID: 6395861
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  • 4. MgATP-independent hydrogen evolution catalysed by nitrogenase: an explanation for the missing electron(s) in the MgADP-AlF4 transition-state complex.
    Yousafzai FK, Eady RR.
    Biochem J; 1999 May 01; 339 ( Pt 3)(Pt 3):511-5. PubMed ID: 10215587
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  • 5. 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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  • 10. 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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  • 12. Evidence on intramolecular electron transfer in the MoFe protein of nitrogenase from Klebsiella pneumoniae from rapid-freeze electron-paramagnetic-resonance studies of its oxidation by ferricyanide.
    Smith BE, Lowe DJ, Chen GX, O'Donnell MJ, Hawkes TR.
    Biochem J; 1983 Jan 01; 209(1):207-13. PubMed ID: 6303301
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  • 13. Nitrogenase of Klebsiella pneumoniae. Kinetics of the dissociation of oxidized iron protein from molybdenum-iron protein: identification of the rate-limiting step for substrate reduction.
    Thorneley RN, Lowe DJ.
    Biochem J; 1983 Nov 01; 215(2):393-403. PubMed ID: 6316927
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