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      https://www.ias.ac.in/article/fulltext/jcsc/108/03/0235-0249

    • Keywords

       

      Iron(III) complexes; X-ray structure; electronic spectra; electron paramagnetic resonance spectra; redox behaviour; dioxygenase activity

    • Abstract

       

      Catechol 1,2-dioxygenase (CTD) and protocatechuate 3,4-dioxygenase (PCD) enzymes catalyse the oxidative cleavage of catechols tocis, cis-muconic acids with the incoporation of molecular oxygen. In our laboratory two series of iron(III) complexes of linear tridentate and tripodal tetradentate phenolate ligands have been characterised using IR, UV-Vis and EPR spectral and electrochemical techniques. The X-ray crystal structure of a few of the complexes have been determined. The interactions of the complexes with a variety of monodentate and bidentate heterocyclic bases as well as phenols have been investigated. The interactions with catecholate anions reveal changes in the phenolate-to-iron(III) charge transfer band, which are remarkably similar to catechol dioxygenase-substrate complexes. The redox behaviour of the complexes and their 1:1 adducts with 3,5-di-t-butylcatechol (H2DBC) has been investigated. All the complexes catalyse the oxidative cleavage of H2DBC by molecular oxygen to yieldcis,cis-muconic anhydride. The structure, redox and catalytic activities of the iron(III) complexes have been discussedvis-a-vis those of the enzymes.

    • Author Affiliations

       

      Mallayan Palaniandavar1 Rathinam Viswanathan1

      1. Department of Chemistry, Bharathidasan University, Tiruchirappalli - 620 024, India
    • Dates

       
  • Journal of Chemical Sciences | News

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