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Articles

Nitrogenase of Klebsiella pneumoniae : electron nuclear double resonance (ENDOR) studies on the substrate reduction site

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B D Howes, K Fisher, D J Lowe
Journal: Biochemical Journal
Biochem J (1994) 297 (2): 261–264.
https://doi.org/10.1042/bj2970261
Published: 15 January 1994
View articletitled, Nitrogenase of Klebsiella pneumoniae : electron nuclear double resonance (ENDOR) studies on the substrate reduction site
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Articles

Klebsiella pneumoniae nitrogenase: pre-steady-state absorbance changes show that redox changes occur in the MoFe protein that depend on substrate and component protein ratio; a role for P-centres in reducing dinitrogen?

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D J Lowe, K Fisher, R N F Thorneley
Journal: Biochemical Journal
Biochem J (1993) 292 (1): 93–98.
https://doi.org/10.1042/bj2920093
Published: 15 May 1993
View articletitled, Klebsiella pneumoniae nitrogenase: pre-steady-state absorbance changes show that redox changes occur in the MoFe protein that depend on substrate and component protein ratio; a role for P-centres in reducing dinitrogen?
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Articles

Klebsiella pneumoniae nitrogenase MoFe protein: chymotryptic proteolysis affects function by limited cleavage of the β -chain and provides high-specific-activity MoFe protein

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K Fisher, D J Lower, R N Pau
Journal: Biochemical Journal
Biochem J (1993) 291 (1): 309–314.
https://doi.org/10.1042/bj2910309
Published: 01 April 1993
View articletitled, Klebsiella pneumoniae nitrogenase MoFe protein: chymotryptic proteolysis affects function by limited cleavage of the β -chain and provides high-specific-activity MoFe protein
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Articles

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

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K Fisher, D J Lowe, R N F Thorneley
Journal: Biochemical Journal
Biochem J (1991) 279 (1): 81–85.
https://doi.org/10.1042/bj2790081
Published: 01 October 1991
View articletitled, 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
Open the PDF for 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 in another window
Articles

Klebsiella pneumoniae nitrogenase. Mechanism of acetylene reduction and its inhibition by carbon monoxide

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D J Lowe, K Fisher, R N F Thorneley
Journal: Biochemical Journal
Biochem J (1990) 272 (3): 621–625.
https://doi.org/10.1042/bj2720621
Published: 15 December 1990
View articletitled, Klebsiella pneumoniae nitrogenase. Mechanism of acetylene reduction and its inhibition by carbon monoxide
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