In Vivo Kinetics of Nitrogenase Formation inClostridium pasteurianum [PDF]
Journal of Bacteriology, 1974 Clostridium pasteurianumexhibits diauxic growth when grown in the presence of both NH3and N2; no nitrogenase activity or formation was detected either serologically or by activity during growth on NH3.
Belinda Seto, L. E. Mortenson
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Role of molybdenum in dinitrogen fixation by Clostridium pasteurianum
Journal of Bacteriology, 1975 The role of Mo in the activity and synthesis of the nitrogenase components of Clostridium pasteurianum has been studied by observing the competition of Mo with its structural analogue W.
J Cardenas, L E Mortenson
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Mechanism of Carbamyl Phosphate Inhibition of Nitrogenase of Clostridium pasteurianum
Journal of Bacteriology, 1974 Carbamyl phosphate caused a maximal inhibition of 50% of the in vitro nitrogenase activity measured by acetylene reduction and dinitrogen reduction.
Belinda L. Seto, L. E. Mortenson
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Transformation of Azotobacter vinelandii strains unable to fix nitrogen with Rhizobium spp. DNA
Canadian Journal of Microbiology (print), 1978 The phenotypes of Azotobacter vinelandii ATCC 12837 strains defective in nitrogen fixation (Nif−) were characterized by intrageneric transformation with known Nif− strains of A. vinelandii OP.
William J. Page
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Proceedings of the National Academy of Sciences of the United States of America, 1972 The electron paramagnetic resonance of nitrogenase components, separately and together with the other reactants in the nitrogenase system (namely, reductant and Mg.ATP), have been examined at low temperatures (
W. Orme-Johnson +6 more
semanticscholar +1 more source
Proceedings of the National Academy of Sciences of the United States of America, 1968 The in vitro reduction of N_2 is a complex process involving at least six different reactants: two proteins [1,2] for which the names azoferredoxin (AzoFd) and molybdoferredoxin (MoFd) have been proposed[3], an electron source, the electron acceptor, ATP[
P. T. Bui, L. Mortenson
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Nitrogenaseless mutants of Azotobacter vinelandii.
Proceedings of the National Academy of Sciences of the United States of America, 1970 Mutants of Azotobacter which grow normally on excess ammonia under a variety of conditions and which grow slowly or not at all on atmospheric nitrogen have been isolated. Extracts of these strains have low or no detectable nitrogenase activity. There are
G. Sorger, D. Trofimenkoff
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Structural Interaction Between Nitrogenase and Cell Membrane in Free-Living, Nitrogen-Fixing Bacteria (Rhodopseudomonas, Viridis, Azotobacter, Vinelandii, Rhodospirillum, Rubrum). [PDF]
, 1982 Rhodopseudomonas viridis grows by means of nitrogen fixation under anaerobic, photosynthetic conditions. In batch culture, nitrogenase activity was highest at early-logarithmic phase, lower during mid- to late-logarithmic phase, and nearly zero during ...
Howard, Karen Smith
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Mapping nif genes of Rhodobacter capsulatus, and characterization of a mutant with a pleiotropic defect in nitrogen metabolism [PDF]
, 1988 Includes vita.Mutations affecting the ability of the photosynthetic bacterium Rhodobacter capsulatus to fix nitrogen (Nif- ) have previously been mapped into six linkage groups (I-VI) by transduction with gene transfer agent (GTA).
Goldenberg, Ann
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Mechanism of the Enzymic Reduction of N_2: The Binding of Adenosine 5'-Triphosphate and Cyanide to the N_2-reducing System [PDF]
, 1968 The in vitro reduction of N_2 is a complex process involving at least six different reactants: two proteins [1,2] for which the names azoferredoxin (AzoFd) and molybdoferredoxin (MoFd) have been proposed[3], an electron source, the electron acceptor, ATP[
Bui, P. T., Mortenson, L. E.
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