Schiff base complex conjugates of bovine serum albumin as artificial metalloenzymes for eco-friendly enantioselective sulfoxidation

Abstract

Artificial metalloenzymes have been prepared by non-covalent insertion of transition metal Schiff-base complexes into bovine serum albumin as the host protein and were characterized by UV-visible spectroscopy, ESI-TOF mass spectrometry and molecular docking studies.

Design of Artificial Enzymes: Insights into Protein Scaffolds

“…Moreover, its mode of action resembled that of some heme enzymes. A similar reactivity can be promoted by Schiff base complexes conjugates with BSA, as reported by Tang and collaborators [107,108] . In detail, they prepared a small library of artificial enzymes, exploiting the non‐covalent conjugation of BSA with different metal‐Schiff base complexes, characterized by the general structure M‐L (where the metal could be Co, Mn, V, Fe or Cr, and the ligand could be 2‐hydroxynaphthalen‐1‐naphthaldehyde and 3,4‐diaminobenzenesulfonic acid).…”

“…A similar reactivity can be promoted by Schiff base complexes conjugates with BSA, as reported by Tang and collaborators. [107,108] In detail, they prepared a small library of artificial enzymes, exploiting the non-covalent conjugation of BSA with different metal-Schiff base complexes, characterized by the general structure M-L (where the metal could be Co, Mn, V, Fe or Cr, and the ligand could be 2-hydroxynaphthalen-1-naphthaldehyde and 3,4-diaminobenzenesulfonic acid). These ArMs were tested on the enantioselective sulfoxidation of differently substituted prochiral thioanisoles, performed in aqueous media and the presence of hydrogen peroxide as oxidant.…”