scholarly journals Comparative organization of nitrogen fixation-specific genes from Azotobacter vinelandii and Klebsiella pneumoniae: DNA sequence of the nifUSV genes.

1987 ◽  
Vol 169 (9) ◽  
pp. 4024-4029 ◽  
Author(s):  
J Beynon ◽  
A Ally ◽  
M Cannon ◽  
F Cannon ◽  
M Jacobson ◽  
...  
Keyword(s):  
Nitrogen Fixation ◽  
Klebsiella Pneumoniae ◽  
Dna Sequence ◽  
Azotobacter Vinelandii

Nitrogen fixation by cell-free extracts of Klebsiella pneumoniae

1968 ◽  
Vol 14 (1) ◽  
pp. 33-38 ◽  
Author(s):  
M. C. Mahl ◽  
P. W. Wilson
Keyword(s):  
Nitrogen Fixation ◽  
Klebsiella Pneumoniae ◽  
Azotobacter Vinelandii ◽  
Ammonium Ion ◽  
Michaelis Constant ◽  
Nitrogen Gas ◽  
Aerobacter Aerogenes ◽  
Free System ◽  
Evolving System ◽  
A Cell

A cell-free system which permits nitrogen fixation by extracts of Klebsiella pneumoniae M5al (formerly Aerobacter aerogenes) has been developed. It is, essentially, that system described by Bulen and associates for Azotobacter vinelandii, utilizing ATP as a source of energy and dithionite as a source of electrons. The Michaelis constant for fixation has been estimated to be 0.12 atm. The extracts possessed an ATP-dependent hydrogen evolving system. Hydrogen evolution from these extracts was less under nitrogen than under helium in the presence of ATP. Nitrogen gas appears to be the inducer of nitrogen fixation. In the absence of N2, no induction of nitrogenase occurs. Nitrogenase is absent in cells grown on NH4+-N. There is a lag of about 13 h after the introduction of N2 gas into a culture which has depleted its supply of NH4+-N before nitrogenase can be detected. For reasons discussed in the text, this conclusion must be regarded as tentative at this time. Ammonium ion appears to prevent the synthesis of new molecules of nitrogenase without affecting the activity of those already formed.

scholarly journals The molybdenum–iron protein of Klebsiella pneumoniae nitrogenase. Evidence for non-identical subunits from peptide ‘mapping’

1976 ◽  
Vol 155 (2) ◽  
pp. 383-389 ◽  
Author(s):  
C Kennedy ◽  
R R. Eady ◽  
E Kondorosi ◽  
D K Rekosh
Keyword(s):  
Amino Acid ◽  
Klebsiella Pneumoniae ◽  
Sodium Dodecyl Sulphate ◽  
Azotobacter Vinelandii ◽  
Peptide Mapping ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Amino Acid Content ◽  
Rhizobium Japonicum ◽  
Fe Protein

The molybdenum- and iron-containing protein components of nitrogenase purified from Klebsiella pneumoniae, Azotobacter vinelandii, Azotobacter chroococcum and Rhizobium japonicum bacteroids all gave either one or two protein-staining bands after sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, depending on the commercial brand of sodium dodecyl sulphate used. The single band obtained with K. pneumoniae Mo-Fe protein when some commercial brands of sodium dodecyl sulphate were used in the preparation of the electrode buffer was resolved into two bands by the addition of 0.01% (v/v) dodecanol to the buffer. Protein extracted from the two bands obtained after electrophoresis of K. pneumoniae Mo-Fe protein gave unique and distinct peptide ‘maps’ after tryptic digestion. Undissociated Mo-Fe protein contained both sets of tryptic peptides. These data are consistent with Mo-Fe protein from K. pneumoniae being composed of non-identical subunits. Amino acid analyses of the subunit proteins revealed some clear differences in amino acid content, but the two subunits showed close compositional relatedness, with a different index [Metzer, H., Shapiro, M.B., Mosiman, J.E. & Vinton, J.G. (1968) Nature (London) 219, 1166-1168] of 4.7.

The flavin transferase ApbE flavinylates the ferredoxin:NAD+-oxidoreductase Rnf required for N2 fixation in Azotobacter vinelandii

2021 ◽  
Author(s):  
Yulia V Bertsova ◽  
Marina V Serebryakova ◽  
Alexander A Baykov ◽  
Alexander V Bogachev
Keyword(s):  
Nitrogen Fixation ◽  
Azotobacter Vinelandii ◽  
Growth Defect ◽  
Deficient Mutant ◽  
Fixed Nitrogen ◽  
Oxidoreductase Activity ◽  
Threonine Residue ◽  
Ferredoxin Reductase ◽  
Relative Contribution ◽  
Fixation System

Abstract Azotobacter vinelandii, the model microbe in nitrogen fixation studies, uses the ferredoxin:NAD+-oxidoreductase Rnf to regenerate ferredoxin (flavodoxin) acting as an electron donor for nitrogenase. However, the relative contribution of Rnf into nitrogenase functioning is unknown because this bacterium contains another ferredoxin reductase, FixABCX. Furthermore, Rnf is flavinylated in the cell, but the importance and pathway of this modification reaction also remain largely unknown. We have constructed A. vinelandii cells with impaired activities of FixABCX and/or putative flavin transferase ApbE. The ApbE-deficient mutant could not produce covalently flavinylated membrane proteins and demonstrated a markedly decreased flavodoxin:NAD+ oxidoreductase activity and significant growth defect under diazotrophic conditions. The double ΔFix/ΔApbE mutation abolished the flavodoxin:NAD+ oxidoreductase activity and the ability of A. vinelandii to grow in the absence of fixed nitrogen source. ApbE flavinylated a truncated RnfG subunit of Rnf1 by forming a phosphoester bond between FMN and a threonine residue. These findings indicate that Rnf (presumably its Rnf1 form) is the major ferredoxin-reducing enzyme in the nitrogen fixation system and that the activity of Rnf depends on its covalent flavinylation by the flavin transferase ApbE.

Nitrogen fixation (acetylene reduction) by Klebsiella pneumoniae in association with 'Park' Kentucky bluegrass (Poa pratensis L.)

1981 ◽  
Vol 27 (1) ◽  
pp. 52-56 ◽  
Author(s):  
L. V. Wood ◽  
R. V. Klucas ◽  
R. C. Shearman
Keyword(s):  
Nitrogen Fixation ◽  
Klebsiella Pneumoniae ◽  
Ethylene Production ◽  
Acetylene Reduction ◽  
Nitrogenase Activity ◽  
Poa Pratensis ◽  
Kentucky Bluegrass ◽  
Surface Sterilization ◽  
Reducing Activity ◽  
Acetylene Reducing Activity

Turfs of 'Park' Kentucky bluegrass reestablished in the greenhouse and inoculated with Klebsiella pneumoniae (W6) showed significantly increased nitrogen fixation (acetylene reduction) compared with control turfs. Mean ethylene production rates per pot were 368 nmol h−1 for K. pneumoniae treated turfs, 55 nmol h−1 for heat-killed K. pneumoniae treated turfs, and 44 nmol h−1 for untreated turfs. Calculated lag periods before activity was observed were generally very short (less than 1 h).When 'Park' Kentucky bluegrass was grown from seed on soil-less medium of Turface, a fired aggregate clay, inoculation with K. pneumoniae (W6) resulted in 9 of 11 turfs showing nitrogenase activity (mean ethylene producion rate per pot was 195 nmol h−1). Only 3 of 11 turfs treated with heat-killed K. pneumoniae showed any activity and their mean rate of ethylene production (40 nmol h−1 per pot) was significantly lower than that for turfs treated with K. pneumoniae.Using the 'Park'–Turface soil-less model system it was shown that acetylene reducing activity was (i) root associated, (ii) generally highest at a depth of 1–4 cm below the surface, (iii) enhanced by washing excised roots, and (iv) inhibited by surface sterilization of excised roots. Klebsiella pneumoniae was recovered from Turface and roots showing acetylene reducing activity.

scholarly journals Effect of Dimethyl Sulphoxide on the Expression of Nitrogen Fixation in Bacteria

1977 ◽  
Vol 30 (2) ◽  
pp. 141 ◽  
Author(s):  
Mary L Skotnicki ◽  
Barry G Rolfe
Keyword(s):  
Escherichia Coli ◽  
Nitrogen Fixation ◽  
Energy Metabolism ◽  
Membrane Proteins ◽  
Klebsiella Pneumoniae ◽  
Dimethyl Sulphoxide ◽  
Rhizobium Trifolii ◽  
Nif Genes ◽  
E Coli ◽  
Selection Of

Storage in dimethyl sulphoxide (DMSO) of Escherichia coli K12 hybrids carrying nif+ genes from Klebsiella pneumoniae can result in selection of a defective nitrogen-fixing phenotype. Similar results are obtained with E. coli K12 hybrids containing the nitrogep-fixing capacity from Rhizobium trifolii. DMSO appears to affect particular inner membrane proteins associated with energy metabolism in E. coli K12 and four chromosomal regions (chID, chlG, his and unc) are associated with resistance to DMSO.

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