A comparison of the heme electronic states in equilibrium and nonequilibrium protein conformations of high-spin ferrous hemoproteins low temperature magnetic circular dichroism studies

Author(s):  
Yurii A. Sharonov ◽  
Nataly A. Sharonova ◽  
Vladimir A. Figlovsky ◽  
Vladimir A. Grigorjev
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.


1981 ◽  
Vol 670 (1) ◽  
pp. 93-100 ◽  
Author(s):  
Andrew J. Thomson ◽  
A.Edward Robinson ◽  
Michael K. Johnson ◽  
Jose J.G. Moura ◽  
Isobel Moura ◽  
...  

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