Electrostatic interactions can strongly increase the efficiency of protein complex formation. The charge distribution in redoxp roteins is often optimizedt os teer ar edox partner to the electron transfer active binding site.T ot est whether the optimizeddistribution is more important than the strength of the electrostatic interactions,anadditional negative patch was introduced on the surface of cytochrome cp eroxidase,a way from the stereospecific binding site,a nd its effect on the encounter complex as well as the rate of complex formation was determined. Monte Carlo simulations and paramagnetic relaxation enhancement NMR experiments indicate that the partner,c ytochrome c, interacts with the new patch.U nexpectedly,t he rate of the active complex formation was not reduced, but rather slightly increased. The findings support the idea that for efficient protein complex formation the strength of the electrostatic interaction is more critical than an optimizedc harge distribution.

Electrostatic interactions can strongly increase the efficiency of protein complex formation. The charge distribution in redoxp roteins is often optimizedt os teer ar edox partner to the electron transfer active binding site.T ot est whether the optimizeddistribution is more important than the strength of the electrostatic interactions,anadditional negative patch was introduced on the surface of cytochrome cp eroxidase,a way from the stereospecific binding site,a nd its effect on the encounter complex as well as the rate of complex formation was determined. Monte Carlo simulations and paramagnetic relaxation enhancement NMR experiments indicate that the partner,c ytochrome c, interacts with the new patch.U nexpectedly,t he rate of the active complex formation was not reduced, but rather slightly increased. The findings support the idea that for efficient protein complex formation the strength of the electrostatic interaction is more critical than an optimizedc harge distribution.