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

      Sabyasachi Sarkar Samar K Das

      Rapid Communication Volume 104 Issue 3 June 1992 pp 437-441

    • Fulltext

       

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      Permanent link:
      https://www.ias.ac.in/article/fulltext/jcsc/104/03/0437-0441

    • 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

       
      Published
      June 1992
      Manuscript received
      3 February 1992

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