Electron Paramagnetic Resonance Analysis of DifferentAzotobacter vinelandiiNitrogenase MoFe-Protein Conformations Generated during Enzyme Turnover:  Evidence forS=3/2Spin States from Reduced MoFe-Protein Intermediates†

Biochemistry ◽  
2001 ◽  
Vol 40 (11) ◽  
pp. 3333-3339 ◽  
Author(s):  
Karl Fisher ◽  
William E. Newton ◽  
David J. Lowe
1983 ◽  
Vol 211 (2) ◽  
pp. 495-497 ◽  
Author(s):  
T R Hawkes ◽  
D J Lowe ◽  
B E Smith

During turnover at 10 degrees C at pH 7.4 in the presence of ethylene, the MoFe protein of Klebsiella pneumoniae nitrogenase (Kp 1) exhibited an electron-paramagnetic-resonance signal with g-values at 2.12, 1.998 and 1.987. 57Fe isotopic substitution demonstrated that this signal arose from the Kp 1 FeMo-cofactor in an S = 1/2 spin state.


2007 ◽  
Vol 101 (9) ◽  
pp. 09H102 ◽  
Author(s):  
A. Ben Mahmoud ◽  
H. J. von Bardeleben ◽  
J. L. Cantin ◽  
E. Chikoidze ◽  
Y. Dumont ◽  
...  

2012 ◽  
Vol 51 (15) ◽  
pp. 8433-8440 ◽  
Author(s):  
Cesare Oliva ◽  
Mattia Allieta ◽  
Marco Scavini ◽  
Cesare Biffi ◽  
Ilenia Rossetti ◽  
...  

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