scholarly journals Evidence for the high-spin heme iron in both stable and unstable reduced forms of lactoperoxidase: low-temperature magnetic circular dichroism data

FEBS Letters ◽  
1995 ◽  
Vol 377 (3) ◽  
pp. 512-514 ◽  
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.


Sign in / Sign up

Export Citation Format

Share Document