Proton NMR and electrophoretic studies of the covalent complex formed by crosslinking yeast cytochrome c peroxidase and horse cytochrome c with water-soluble carbodiimide

Biochemistry ◽  
1987 ◽  
Vol 26 (13) ◽  
pp. 3821-3826 ◽  
Author(s):  
Susan J. Moench ◽  
James D. Satterlee ◽  
James E. Erman
Biochemistry ◽  
1992 ◽  
Vol 31 (14) ◽  
pp. 3661-3670 ◽  
Author(s):  
Susan J. Moench ◽  
Stamatia Chroni ◽  
Bih Show Lou ◽  
James E. Erman ◽  
James D. Satterlee

1986 ◽  
Vol 239 (2) ◽  
pp. 333-337 ◽  
Author(s):  
A E Proudfoot ◽  
C J Wallace ◽  
D E Harris ◽  
R E Offord

We have prepared a semisynthetic analogue of fully acetimidylated horse cytochrome c, a complex in which the peptide bond between residues glycine-37 and arginine-38 is lacking. In contrast with the complex that we have previously described [Harris & Offord (1977) Biochem. J. 161, 12-25], in which the break in continuity is between residues arginine-38 and lysine-39, the new analogue has a nearly normal redox potential, and can more fully restore succinate oxidation to mitochondria depleted of cytochrome c. Studies of this and other analogues lead us to propose an explanation for the low biological activity of complex (1-38)-(39-104) and a role for the invariance of arginine-38.


1994 ◽  
Vol 224 (1) ◽  
pp. 81-87 ◽  
Author(s):  
James D. Satterlee ◽  
Steve L. Alam ◽  
J. Matthew Mauro ◽  
James E. Erman ◽  
Thomas L. Poulos

FEBS Letters ◽  
1986 ◽  
Vol 194 (1) ◽  
pp. 73-77 ◽  
Author(s):  
Helena Santos ◽  
David L. Turner

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