Enhanced Arylamine N-Oxygenase Activity of Polymer-Enzyme Assemblies by Facilitating Electron-Transferring Efficiency

Biomacromolecules. 2018 Mar 12;19(3):918-925. doi: 10.1021/acs.biomac.7b01706. Epub 2018 Feb 28.

Abstract

A novel N-oxygenase-coated core-shell nanoparticle was generated through the coassembly of poly(4-vinylpyridine) (P4VP) and arylamine N-oxygenase CmlI. The resulting enzyme-hybridized particles, P4VP-CmlI, showed excellent catalytic activities on the oxidation of two arylamine substrates, i.e., p-aminophenol ( pAP) and p-aminobenzoic acid ( pABA), using a surrogate redox system or a peroxide shunt as co-oxidants. In comparison with the free enzyme, P4VP-CmlI particles exhibited a significantly enhanced catalytic efficiency when using pyridine nucleotide (NADH) and proper redox mediators. Products at different oxygenation stages were observed. On the contrary, the activity of the enzyme-containing nanoparticles was very similar to the free enzyme when using the peroxide shunt. The enhanced catalytic efficiency of the P4VP-CmlI assemblies is attributed to a more efficient electron delivery.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Bacterial Proteins / chemistry*
  • Biocatalysis
  • Electrons*
  • Enzyme Stability
  • Mixed Function Oxygenases / chemistry*
  • Polyvinyls / chemistry*
  • Streptomyces / enzymology*
  • Substrate Specificity

Substances

  • Bacterial Proteins
  • Polyvinyls
  • poly(4-vinylpyridine)
  • Mixed Function Oxygenases
  • arylamine N-hydroxylase