Kinetic Studies on Klebsiella pneumoniae Nitrogenase
نویسندگان
چکیده
منابع مشابه
Nitrogenase of Klebsiella pneumoniae
1. Nitrogenase from the facultative anaerobe Klebsiellapneumoniae was resolved into two protein components resembling those obtained from other nitrogen-fixing bacteria. 2. Both proteins were purified to homogeneity as shown by the criteria of disc electrophoresis and ultracentrifugal analysis. 3. The larger component had a mol.wt. of 218000 and contained one Mo atom, 17Fe atoms and 17 acid-lab...
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Blumberg, W. E. & Peisach, J. (1974) Arch. Biochem. Biophys. 162,502-512 Cammack, R. (1973) Biochem. Biophys. Res. Commun. 54,548-554 Cammack, R., Rao, K. K. & Hall, D. 0. (1971) Biochem. Biophys. Res. Commun. 44,s-14 Coffman, R. E. & Stavens, B. W. (1970) Biochem. Biophys. Res. Commun. 41,163-169 Fee, J. A. & Palmer, G. (1971) Biochim. Biophys. Actu 249,175-195 Genonde, Ic, Schlaak, M. E., Bri...
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Proton electron nuclear double resonance (ENDOR) spectra from the iron-molybdenum cofactor (FeMoco) of Klebsiella pneumoniae nitrogenase bound to the enzyme show that a wide variety of substrates and inhibitors, including dinitrogen, acetylene and cyanide, do not bind at or close to FeMoco in the dithionite-reduced state of the free MoFe protein, in agreement with our previous kinetic studies. ...
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Klebsiella pneumoniae does not fix N(2) under aerobic conditions. The two protein components required for nitrogenase activity were studied during aeration of cells in nitrogen-free media. Component II of nitrogenase was inactivated more slowly in vivo than component I during aeration. The rate of loss of component II was less than the rate of component II synthesis during derepression. No inac...
متن کاملNitrogenase from nifV mutants of Klebsiella pneumoniae contains an altered form of the iron-molybdenum cofactor.
When the iron-molybdenum cofactor (FeMoco) was extracted from the MoFe protein of nitrogenase from a nifV mutant of Klebsiella pneumoniae and combined with the FeMoco-deficient MoFe protein from a nifB mutant, the resultant MoFe protein exhibited the NifV phenotype, i.e. in combination with wild-type Fe protein it exhibited poor N2-fixation activity and its H2-evolution activity was inhibited b...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 1971
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.68.9.2016