Circular Dichroism and Magnetic Circular Dichroism Studies of the Mixed-Valence Binuclear Non-Heme Iron Active Site in Uteroferrin and Its Anion Complexes

1997 ◽  
Vol 119 (49) ◽  
pp. 11832-11842 ◽  
Author(s):  
Yi-Shan Yang ◽  
James M. McCormick ◽  
Edward I. Solomon

1973 ◽  
Vol 51 (4) ◽  
pp. 1054-1061 ◽  
Author(s):  
D.D. Ulmer ◽  
B. Holmquist ◽  
B.L. Vallee




2016 ◽  
Vol 69 ◽  
pp. 42-46 ◽  
Author(s):  
J. Wang ◽  
L. Liang ◽  
L.T. Zhang ◽  
M. Yano ◽  
K. Terashima ◽  
...  


1976 ◽  
Vol 159 (3) ◽  
pp. 811-813 ◽  
Author(s):  
T Brittain ◽  
J Springall ◽  
C Greenwood ◽  
A J Thomson

The spin states of the haem components of mixed-valence cytochrome oxidase were studied at room temperature and at temperature down to 20K by using magnetic circular dichroism. The room-temperature studies show the presence of a low-spin ferrous haem together with a low-spin ferric haem, which we attribute to heams a3 and a respectively. At temperatures below 100K it appears that the CO of the mixed-valence CO complex may be irreversibly photolysed, and that in this case haems a and a3 assume their high-spin states. Thus in this enzyme haem-haem interactions appear possible at temperatures below 100K.



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