Electrochemical characterization of the iron-molybdenum cofactor from Azotobacter vinelandii nitrogenase

1985 ◽  
Vol 107 (19) ◽  
pp. 5364-5368 ◽  
Author(s):  
Franklin A. Schultz ◽  
Stephen F. Gheller ◽  
Barbara K. Burgess ◽  
Samuel Lough ◽  
William E. Newton
Keyword(s):  
Azotobacter Vinelandii ◽  
Molybdenum Cofactor ◽  
Electrochemical Characterization ◽  
Iron Molybdenum Cofactor

Spectroscopic Characterization of the Isolated Iron-Molybdenum Cofactor (FeMoco) Precursor from the Protein NifEN

2011 ◽  
Vol 123 (34) ◽  
pp. 7933-7936 ◽  
Author(s):  
Aaron W. Fay ◽  
Michael A. Blank ◽  
Chi Chung Lee ◽  
Yilin Hu ◽  
Keith O. Hodgson ◽  
...  
Keyword(s):  
Spectroscopic Characterization ◽  
Molybdenum Cofactor ◽  
Iron Molybdenum Cofactor

scholarly journals Purification and Characterization of NafY (Apodinitrogenase γ Subunit) fromAzotobacter vinelandii

2004 ◽  
Vol 279 (19) ◽  
pp. 19739-19746 ◽  
Author(s):  
Luis M. Rubio ◽  
Steven W. Singer ◽  
Paul W. Ludden
Keyword(s):  
Biochemical Characterization ◽  
Azotobacter Vinelandii ◽  
Site Directed Mutagenesis ◽  
Cofactor Binding ◽  
Unknown Structure ◽  
Additional Protein ◽  
Epr Signal ◽  
Iron Molybdenum Cofactor ◽  
Very High

The formation of an active dinitrogenase requires the synthesis and the insertion of the iron-molybdenum cofactor (FeMo-co) into a presynthesized apodinitrogenase. InAzotobacter vinelandii, NafY (also known as γ protein) has been proposed to be a FeMo-co insertase because of its ability to bind FeMo-co and apodinitrogenase. Here we report the purification and biochemical characterization of NafY and reach the following conclusions. First, NafY is a 26-kDa monomeric protein that binds one molecule of FeMo-co with very high affinity (Kd≈ 60 nm); second, the NafY-FeMo-co complex exhibits aS= 3/2 EPR signal with features similar to the signals for extracted FeMo-co and the M center of dinitrogenase; third, site-directed mutagenesis ofnafYindicates that the His121residue of NafY is involved in cofactor binding; and fourth, NafY binding to apodinitrogenase or to FeMo-co does not require the presence of any additional protein. In addition, we have obtained evidence that suggests the ability of NafY to bind NifB-co, an FeS cluster of unknown structure that is a biosynthetic precursor to FeMo-co.

scholarly journals Spectroscopic Characterization of the Isolated Iron-Molybdenum Cofactor (FeMoco) Precursor from the Protein NifEN

2011 ◽  
Vol 50 (34) ◽  
pp. 7787-7790 ◽  
Author(s):  
Aaron W. Fay ◽  
Michael A. Blank ◽  
Chi Chung Lee ◽  
Yilin Hu ◽  
Keith O. Hodgson ◽  
...  
Keyword(s):  
Spectroscopic Characterization ◽  
Molybdenum Cofactor ◽  
Iron Molybdenum Cofactor

scholarly journals Small-angle x-ray scattering studies of the iron-molybdenum cofactor from Azotobacter vinelandii nitrogenase.

1993 ◽  
Vol 268 (28) ◽  
pp. 20953-20957
Author(s):  
D Eliezer ◽  
P Frank ◽  
N Gillis ◽  
W.E. Newton ◽  
S Doniach ◽  
...  
Keyword(s):  
Small Angle ◽  
Azotobacter Vinelandii ◽  
Molybdenum Cofactor ◽  
X Ray ◽  
X Ray Scattering ◽  
Iron Molybdenum Cofactor ◽  
Ray Scattering

Solubilization of the iron molybdenum cofactor of Azotobacter vinelandii nitrogenase in dimethylformamide and acetonitrile

1986 ◽  
Vol 139 (2) ◽  
pp. 740-746 ◽  
Author(s):  
Samuel M. Lough ◽  
Deloria L. Jacobs ◽  
Dorothy M. Lyons ◽  
Gerald D. Watt ◽  
John W. McDonald
Keyword(s):  
Azotobacter Vinelandii ◽  
Molybdenum Cofactor ◽  
Iron Molybdenum Cofactor
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