• Synthesis of the active sites of molybdoenzymes: MoO2(VI) and MoO(IV)-dithiolene complexes mimicking enzymatic reactions of sulphite oxidase with saturation kinetics

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    • Keywords


      Sulphite oxidase; proton coupled electron transfer; saturation kinetics; inhibition; functional analogues; trimethylamine N-oxide reductase

    • Abstract


      [MoVIO2(S2C2(CN)2)2]2− (┘1) and [MoIVO(S2C2(CN)2)2]2− (2) mimick oxidoreductase enzymatic activities of sulphite oxidase with biological electron donor, SO32−, andin vitro electron acceptor, [Fe(CN)6]3−, demonstrating proton coupled electron transfer reaction in water and inhibition of the oxidation of (2) in the presence of KCN. The sulphite exidizing system is characterized by substrate saturation kinetics indicating the biological significance of the reactions

    • Author Affiliations


      Sabyasachi Sarkar1 Samar K Das1

      1. Department of Chemistry, Indian Institute of Technology, Kanpur - 208 016, India
    • Dates

  • Journal of Chemical Sciences | News

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