Document Detail


Nitrogen fixation system of tungsten-resistant mutants of Azotobacter vinelandii.
MedLine Citation:
PMID:  6956567     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Mutants of Azotobacter vinelandii ATCC 12837 were isolated which could fix N2 in the presence of high tungsten concentrations. The most studied of these mutants (WD2) grew well in N-free modified Burk broth containing 10 mM W, whereas the wild type would not grow in this medium. WD2 would also grow in Burk N-free broth at about the same rate as the wild type. WD2 in broth containing W exhibited 22% of the whole cell acetylene reduction activity of the wild type in broth containing Mo and showed a lowered affinity for acetylene. Two-dimensional gel electrophoresis experiments showed that N2-fixing cells of WD2 from broth containing W or Mo did not produce significant amounts of component I of native nitrogenase protein. Electron spin resonance spectra of whole cells and cell-free extracts of WD2 from broth containing W lacked any trace of the g = 3.6 resonance associated with FeMoCo.
Authors:
G D Riddle; J G Simonson; B J Hales; H D Braymer
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of bacteriology     Volume:  152     ISSN:  0021-9193     ISO Abbreviation:  J. Bacteriol.     Publication Date:  1982 Oct 
Date Detail:
Created Date:  1982-12-03     Completed Date:  1982-12-03     Revised Date:  2010-09-10    
Medline Journal Info:
Nlm Unique ID:  2985120R     Medline TA:  J Bacteriol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  72-80     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Acetylene / metabolism
Azotobacter / drug effects,  genetics,  metabolism*
Drug Resistance, Microbial
Molybdenum / pharmacology
Mutation
Nitrogen Fixation*
Nitrogenase / analysis
Oxidation-Reduction
Tungsten / pharmacology*
Chemical
Reg. No./Substance:
74-86-2/Acetylene; 7439-98-7/Molybdenum; 7440-33-7/Tungsten; EC 1.18.6.1/Nitrogenase
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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