The structural and functional role of lysine residues in the binding domain of cytochrome c in the electron transfer to cytochrome c oxidase

1999 ◽  
Vol 261 (2) ◽  
pp. 379-391 ◽  
Author(s):  
Susanne Dopner ◽  
Peter Hildebrandt ◽  
Federico I. Rosell ◽  
A. Grant Mauk ◽  
Matthias von Walter ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Functional Role ◽  
Binding Domain ◽  
Lysine Residues

Role of positive charge of lysine residue on cytochrome c3 for electrostatic interaction with hydrogenase

2007 ◽  
Vol 11 (01) ◽  
pp. 66-73
Author(s):  
Shin Iida ◽  
Noriyuki Asakura ◽  
Kenji Tabata ◽  
Ichiro Okura ◽  
Toshiaki Kamachi
Keyword(s):  
Electron Transfer ◽  
Cytochrome C ◽  
Hydrogen Evolution ◽  
Electrostatic Interaction ◽  
Positive Charge ◽  
Lysine Residue ◽  
Site Directed Mutagenesis ◽  
Desulfovibrio Vulgaris ◽  
Lysine Residues

Cytochrome c3 from Desulfovibrio vulgaris (Miyazaki) is an electron transfer protein containing four hemes per molecule. Its physiological electron transfer partner is the hydrogenase which catalyzes reversible oxidation of hydrogen. The complex formation between cytochrome c3 and hydrogenase is caused by electrostatic interaction, because cytochrome c3 is a basic protein and hydrogenase is an acidic protein. As cytochrome c3 has 20 lysine residues among 108 amino acids, the positive charges of some lysine residues may play an important role in the interaction with hydrogenase. To clarify the role of positive charge of lysine residue, the positive charge was changed to neutral or negative charge using chemical modification and site-directed mutagenesis. When the positive charges around heme IV were changed, the hydrogen evolution rate with hydrogenase decreased. The affinity between hydrogenase and mutated cytochrome c3 (K57Q, K57E, K72Q, K94Q, K94E) were not affected. On the other hand, the affinity of K72E cytochrome c3 for hydrogenase was very low. These results suggest that the positive charge around heme IV plays an important role in the electrostatic interaction with hydrogenase in hydrogen evolution.

scholarly journals Role of tryptophan 121 in the soluble CuA domain of cytochrome c oxidase: structure and electron transfer studies

2003 ◽  
Vol 16 (6) ◽  
pp. 435-441 ◽  
Author(s):  
A.-X. Song ◽  
L.-Z. Li ◽  
T. Yu ◽  
S.-M. Chen ◽  
Z.-X. Huang
Keyword(s):  
Electron Transfer ◽  
Cytochrome C ◽  
Cytochrome C Oxidase
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