[Evaluation of effect of the peptide structure on energetics of reduction-oxidation reactions of proteins containing Fe4S4 clusters in computer experiments].

The methods of molecular dynamics were used to study the influence of peptide matrix and conformational relaxation on the thermal effects of redox reactions of two proteins containing Fe4S4 clusters with sharply differing redox potential values. It was shown that the depth of immersion of the Fe4S4 cluster in the protein globule affects the parameters of chemical equilibrium. It was found that the peptide matrix makes a determining contribution to the compensation of the Coulomb repulsion energy in Fe4S4 clusters.