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Effect of paraoxon on the conformation of human serum albumin redox site with different oxidation states of Cys34 according to molecular modeling data. (A–C)—paraoxon is bound in Sudlow site I; (D–F)—is bound in Sudlow site II; (A,D)—Cys34 is reduced (Cys34-SH); (B,E)—Cys34 is oxidised to sulfenic acid (Cys34-SOH); (C,F)—Cys34 is oxidised to sulfinic acid (Cys34-S(O)O−).
