Switching engineered Vitreoscilla hemoglobin into carbene transferase for enantioselective SH insertion

Int J Biol Macromol. 2024 Oct;278(Pt 2):134756. doi: 10.1016/j.ijbiomac.2024.134756. Epub 2024 Aug 13.

Abstract

An attractive strategy for efficiently forming CS bonds is through the use of diazo compounds SH insertion. However, achieving good enantioselective control in this reaction within a biocatalytic system has proven to be challenging. This study aimed to enhance the activity and enantioselectivity of to enable asymmetric SH insertion. The researchers conducted site-saturation mutagenesis (SSM) on 5 amino acid residues located around the iron carbenoid intermediate within a distance of 5 Å, followed by iterative saturation mutagenesis (ISM) of beneficial mutants. Through this process, the beneficial variant VHbSH(P54R/V98W) was identified through screening with 4-(methylmercapto) phenol as the substrate. This variant exhibited up to 4-fold higher catalytic efficiency and 6-fold higher enantioselectivity compared to the wild-type VHb. Computational studies were also conducted to elucidate the detailed mechanism of this asymmetric SH insertion, explaining how active-site residues accelerate this transformation and provide stereocontrol.

Keywords: Asymmetric synthesis; Carbene-transferase; S-H insertion; Semi-rational design; Vitreoscilla hemoglobin.

MeSH terms

  • Bacterial Proteins* / chemistry
  • Bacterial Proteins* / genetics
  • Bacterial Proteins* / metabolism
  • Biocatalysis
  • Catalytic Domain
  • Methane / analogs & derivatives
  • Methane / chemistry
  • Methane / metabolism
  • Models, Molecular
  • Mutagenesis, Site-Directed
  • Protein Engineering* / methods
  • Stereoisomerism
  • Substrate Specificity
  • Truncated Hemoglobins* / chemistry
  • Truncated Hemoglobins* / genetics
  • Truncated Hemoglobins* / metabolism

Substances

  • Truncated Hemoglobins
  • Bacterial Proteins
  • hemoglobin protein, Vitreoscilla
  • carbene
  • Methane