Time-resolved UV-vis spectroelectrochemical studies of the electron transfer process of cytochrome c

2000 ◽  
Vol 45 (18) ◽  
pp. 2877-2881 ◽  
Author(s):  
L.L. Wu ◽  
H.G. Huang ◽  
J.X. Li ◽  
J. Luo ◽  
Z.H. Lin
2013 ◽  
Vol 117 (20) ◽  
pp. 10308-10314 ◽  
Author(s):  
Rudi Agus Setiawan ◽  
Hiromasa Nishikiori ◽  
Yohei Uesugi ◽  
Kyohei Miyashita ◽  
Mostafa A. El-Sayed ◽  
...  

Science ◽  
1988 ◽  
Vol 240 (4850) ◽  
pp. 311-313 ◽  
Author(s):  
N Liang ◽  
AG Mauk ◽  
GJ Pielak ◽  
JA Johnson ◽  
M Smith ◽  
...  

Yeast iso-1-cytochrome c (Cc) mutants have been constructed with Phe, Tyr, Gly, Ser, Leu, and Ile at position 82, each with Thr substituted for Cys at position 102. Their long-range electron transfer with zinc-substituted cytochrome c peroxidase (ZnCcP) has been studied by two kinetic techniques. The charge-separated complex, [(ZnCcP)+,FeIICc] converts to [ZnCcP,FeIIICc] by a single, intracomplex electron transfer step that is not governed by "gating" through possible rapid dissociation of the complex or isomerization (for example, heme-ligand) by FeIICc subsequent to its formation from FeIIICc. In every variant with an aliphatic residue at position 82 of Cc, the rate of this electron transfer process is approximately 10(4) slower at approximately 0 degrees C than for the two variants with aromatic residues.


2003 ◽  
Vol 32 (5) ◽  
pp. 450-451 ◽  
Author(s):  
Hiroyuki Ohno ◽  
Chiiko Suzuki ◽  
Kenta Fukumoto ◽  
Masahiro Yoshizawa ◽  
Kyoko Fujita

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