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Rationally designed molecules for resurgence of cyanide mitigated cytochrome c oxidase activity.
Bioorganic Chemistry 2018 October 26
Cytochrome c oxidase (CcOX) containing binuclear heme a3 -Cu B centre (BNC) mechanises the process of electron transfer in the last phase of cellular respiration. The molecular modelling based structural analysis of CcOX - heme a3 -Cu B complex was performed and the disturbance to this complex under cyanide poisoning conditions was investigated. Taking into consideration the results of molecular docking studies, new chemical entities were developed for clipping cyanide from the enzyme and restoring its normal function. It was found that the molecules obtained by combining syringaldehyde, oxindole and chrysin moieties bearing propyl/butyl spacing groups occupy the BNC region and effectively remove cyanide bound to the enzyme. The binding constant of compound 2 with CN- was 2.3 × 105 M-1 and its ED50 for restoring the cyanide bound CcOX activity in 10 min was 16 µM. The compound interacted with CN- over the pH range 5-10. The comparison of the loss of enzymatic activity in the presence of CN- and resumption of enzymatic activity by compound 2 mediated removal of CN- indicated the efficacy of the compound as antidote of cyanide.
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