Characterization of an Fe4S4 (?P?) cluster containing species from the nitrogenase MoFe protein ofAzotobacter vinelandii

1991 ◽  
Vol 78 (10) ◽  
pp. 460-462 ◽  
Author(s):  
A. M�ller ◽  
K. Kn�ttel ◽  
E. Krickemeyer ◽  
A. Hildebrand ◽  
H. B�gge ◽  
...  
Keyword(s):  
Mofe Protein ◽  
Ofazotobacter Vinelandii

Characterization of a FeMo cofactor-deficient MoFe protein from anifE-deleted strain (DJ35) ofAzotobacter vinelandii

2005 ◽  
Vol 50 (20) ◽  
pp. 2305-2310
Author(s):  
Ying Zhao ◽  
Shaomin Bian ◽  
Chunxi Zhang ◽  
Huina Zhou ◽  
Huangping Wang ◽  
...  
Keyword(s):  
Mofe Protein ◽  
Femo Cofactor ◽  
Ofazotobacter Vinelandii

Characterization of the pyoverdines ofAzotobacter vinelandii ATCC 12 837 with regard to heterogeneity

1991 ◽  
Vol 4 (4) ◽  
pp. 223-232 ◽  
Author(s):  
Nick Menhart ◽  
Abraham Thariath ◽  
Thammiah Viswanatha
Keyword(s):  
Ofazotobacter Vinelandii

Isolation and partial characterization of siderophore mutants ofAzotobacter vinelandii

1988 ◽  
Vol 17 (6) ◽  
pp. 343-346 ◽  
Author(s):  
Bernard R. Glick ◽  
Nick Menhart ◽  
Nei W. Soong ◽  
Wendy H. Farmer ◽  
T. Viswanatha ◽  
...  
Keyword(s):  
Partial Characterization ◽  
Ofazotobacter Vinelandii

scholarly journals Isolation and characterization of oxygen sensitive mutants ofAzotobacter vinelandii

1991 ◽  
Vol 77 (1) ◽  
pp. 73-78 ◽  
Author(s):  
Hitoshi Iwahashi ◽  
Yoshinobu Hachiya ◽  
Junichiro Someya
Keyword(s):  
Isolation And Characterization ◽  
Oxygen Sensitive ◽  
Ofazotobacter Vinelandii

scholarly journals Isolation and characterization of R-primes ofAzotobacter vinelandii

1991 ◽  
Vol 80 (2-3) ◽  
pp. 213-216 ◽  
Author(s):  
G. Blanco ◽  
J.C. Gutierrez ◽  
F. Ramos ◽  
M. Tortolero
Keyword(s):  
Isolation And Characterization ◽  
Ofazotobacter Vinelandii

scholarly journals Purification and characterization of the inactive MoFe protein (NifB-Kp1) of the nitrogenase from nifB mutants of Klebsiella pneumoniae

1983 ◽  
Vol 209 (1) ◽  
pp. 43-50 ◽  
Author(s):  
T R Hawkes ◽  
B E Smith
Keyword(s):  
Klebsiella Pneumoniae ◽  
Double Mutant ◽  
Specific Activity ◽  
Equimolar Amount ◽  
Wild Type ◽  
Purification And Characterization ◽  
Point Mutant ◽  
Mofe Protein ◽  
Iron Molybdenum Cofactor

The inactive MoFe protein of nitrogenase, NifB-Kp1, from two distinct nifB mutants of Klebsiella pneumoniae, Kp5058 (a nifB point mutant) and UNF1718 (a nifB, nifJ double mutant) has been purified and characterized. NifB-Kp1 can be activated by reaction with the iron-molybdenum cofactor, FeMoco, extracted from active MoFe protein. NifB-Kp1 purified from either source had similar properties and was contaminated with an approximately equimolar amount of protein of mol.wt. 21 000. Like active wild-type Kp1, it was an alpha 2 beta 2 tetramer, but it was far less stable than Kp1, deteriorating rapidly at temperatures above 8 degrees C or on mild oxidation. NifB-Kp1 preparations contained 0.4-0.9 Mo and 9.0 +/- 0.9 Fe atoms . mol-1 and, when activated by FeMoco, had a specific activity of approx. 500 units . mg-1. The Mo in our preparations was not associated with the e.p.r. signal normally observed from FeMoco. All preparations exhibited a weak gav. = 1.95 e.p.r. signal which was probably not associated with activatable protein.

Purification and characterization of a FeMo cofactor-deficient MoFe protein

Biochemistry ◽  
1994 ◽  
Vol 33 (39) ◽  
pp. 11842-11849 ◽  
Author(s):  
Narasaiah Gavini ◽  
Li Ma ◽  
Gerald Watt ◽  
Barbara K. Burgess
Keyword(s):  
Purification And Characterization ◽  
Mofe Protein ◽  
Femo Cofactor

Morphological Characterization of Mycobacteriophage R1

1974 ◽  
Vol 32 ◽  
pp. 254-255
Author(s):  
B. L. Soloff ◽  
T. A. Rado
Keyword(s):  
Carbon Source ◽  
Stationary Phase ◽  
Growth Phase ◽  
Minimal Medium ◽  
Morphological Characterization ◽  
Logarithmic Growth Phase ◽  
Complete Lysis ◽  
Lysogenic Culture ◽  
Logarithmic Growth

Mycobacteriophage R1 was originally isolated from a lysogenic culture of M. butyricum. The virus was propagated on a leucine-requiring derivative of M. smegmatis, 607 leu−, isolated by nitrosoguanidine mutagenesis of typestrain ATCC 607. Growth was accomplished in a minimal medium containing glycerol and glucose as carbon source and enriched by the addition of 80 μg/ ml L-leucine. Bacteria in early logarithmic growth phase were infected with virus at a multiplicity of 5, and incubated with aeration for 8 hours. The partially lysed suspension was diluted 1:10 in growth medium and incubated for a further 8 hours. This permitted stationary phase cells to re-enter logarithmic growth and resulted in complete lysis of the culture.

AEM analysis of crystallization in Ti-based amorphous alloys

1983 ◽  
Vol 41 ◽  
pp. 270-271
Author(s):  
A.R. Pelton ◽  
A.F. Marshall ◽  
Y.S. Lee
Keyword(s):  
Magnetic Properties ◽  
Amorphous Alloys ◽  
Amorphous Materials ◽  
Isothermal Annealing ◽  
Amorphous Matrix ◽  
Nucleation And Growth ◽  
Current Interest ◽  
Amorphous Films ◽  
Electrical And Magnetic Properties

Amorphous materials are of current interest due to their desirable mechanical, electrical and magnetic properties. Furthermore, crystallizing amorphous alloys provides an avenue for discerning sequential and competitive phases thus allowing access to otherwise inaccessible crystalline structures. Previous studies have shown the benefits of using AEM to determine crystal structures and compositions of partially crystallized alloys. The present paper will discuss the AEM characterization of crystallized Cu-Ti and Ni-Ti amorphous films.Cu60Ti40: The amorphous alloy Cu60Ti40, when continuously heated, forms a simple intermediate, macrocrystalline phase which then transforms to the ordered, equilibrium Cu3Ti2 phase. However, contrary to what one would expect from kinetic considerations, isothermal annealing below the isochronal crystallization temperature results in direct nucleation and growth of Cu3Ti2 from the amorphous matrix.

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