The dependence of biological electron transfer rates on exothermicity. The cytochrome c/cytochrome b5 couple

1985 ◽  
Vol 107 (26) ◽  
pp. 7811-7816 ◽  
Author(s):  
George McLendon ◽  
John R. Miller
2000 ◽  
Vol 267 (4) ◽  
pp. 950-954 ◽  
Author(s):  
Ole Farver ◽  
Ólöf Einarsdóttir ◽  
Israel Pecht

2005 ◽  
Vol 392 (3) ◽  
pp. 583-587 ◽  
Author(s):  
Chantal Capeillere-Blandin ◽  
Delphine Mathieu ◽  
Daniel Mansuy

We previously showed that one-electron transfer from tetrahydropterins to iron porphyrins is a very general reaction, with formation of an intermediate cation radical similar to the one detected in NO synthase. As a model reaction, the rates of reduction of eight haemoproteins by diMePH4 (6,7-dimethyltetrahydropterin) have been studied and correlated with their one-electron reduction potentials, Em (FeIII/FeII). On the basis of kinetic data analyses, a bimolecular collisional mechanism is proposed for the electron transfer from diMePH4 to ferrihaemoproteins. Haemoproteins with reduction potentials below −160 mV were shown not to be reduced by diMePH4 to the corresponding ferrohaemoproteins. For haemoproteins with reduction potentials more positive than −160 mV, such as chloroperoxidase, cytochrome b5, methaemoglobin and cytochrome c, there was a good correlation between the second-order reduction rate constant and the redox potential, Em (FeIII/FeII):The rate of reduction of cytochrome c by BH4 [(6R)-5,6,7,8-tetrahydrobiopterin] was determined to be similar to that of the reduction of cytochrome c by diMePH4. These results confirm the role of tetrahydropterins as one-electron donors to FeIII porphyrins.


1991 ◽  
Vol 194 (1) ◽  
pp. 311-316 ◽  
Author(s):  
Ling Qin ◽  
Karla K. Rodgers ◽  
Stephen G. Sligar

Biochemistry ◽  
1993 ◽  
Vol 32 (2) ◽  
pp. 622-627 ◽  
Author(s):  
T. E. Meyer ◽  
M. Rivera ◽  
F. A. Walker ◽  
M. R. Mauk ◽  
A. G. Mauk ◽  
...  

1997 ◽  
Vol 67 (1-4) ◽  
pp. 405
Author(s):  
Yu-Long Sun ◽  
Yun-Hua Wang ◽  
Man-Ming Yan ◽  
Yi Xie ◽  
Zhong-Xian Huang

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