Scientists Uncover High-Resolution Structure of SOI Enzyme for Biocatalysis

Researchers at the Paul Scherrer Institute (PSI) have determined the high-resolution structures of the styrene oxide isomerase (SOI) enzyme, a membrane-bound protein produced by bacteria, revealing its unique catalytic mechanism and ferric haem b prosthetic group, which has the potential to revolutionize the chemical and pharmaceutical industries by enabling energy-saving and environmentally friendly production of precursors for drugs and important chemicals. This description focuses on the primary topic of the article (the discovery of the SOI enzyme's structure and mechanism), the main entities involved (researchers at PSI and the SOI enzyme), the context (industrial biocatalysis and Meinwald rearrangements), and the significant implications (revolutionizing the chemical and pharmaceutical industries). The description also provides objective and relevant details that will help an AI generate an accurate visual representation of the article's content, such as the enzyme's membrane-bound structure and ferric haem b prosthetic group.

author-image
Bijay Laxmi
New Update
Scientists Uncover High-Resolution Structure of SOI Enzyme for Biocatalysis

Scientists Uncover High-Resolution Structure of SOI Enzyme for Biocatalysis

Researchers have determined the high-resolution structures of the styrene oxide isomerase (SOI) enzyme, revealing its unique catalytic mechanism and ferric haem b prosthetic group. This breakthrough, published in the journal Nature Chemistry on May 14, 2024, provides insights into industrial biocatalysis and Meinwald rearrangements.

Why this matters: This discovery has the potential to revolutionize the chemical and pharmaceutical industries by enabling the production of precursors for drugs and important chemicals under energy-saving and environmentally friendly conditions. Furthermore, the enzyme's stability and specificity make it a valuable tool for large-scale industrial applications, contributing to a more sustainable and circular economy.

The SOI enzyme, a membrane-bound protein discovered decades ago and produced by bacteria, catalyzes the isomerization of aryl epoxides to carbonyl compounds under physiological conditions. It is the only known bacterial enzyme to catalyze the Meinwald reaction, a Lewis acid-catalyzed isomerization of an epoxide to a carbonyl compound.

The study, conducted by researchers at the Paul Scherrer Institute (PSI) in part at the Swiss Light Source SLS using cryo-electron microscopy, found that the enzyme's catalytic mechanism involves ferric haem b bound at the subunit interface of the trimeric enzyme, which acts as a Lewis acid by binding to the epoxide oxygen. "The enzyme is an impressive example of how nature makes chemical reactions possible in a simple and ingenious way," said Xiaodan Li, one of the researchers.

The high regio selectivity and stereo specificity of SOI are explained by the positioning of substrates in a hydrophobic pocket. "It is so far the only bacterial enzyme known to catalyze the Meinwald reaction," noted Richard Kammerer, another researcher involved in the study. The enzyme's specificity is particularly important for generating precursor molecules for drugs.

The findings can support extending the range of epoxide substrates and potentially repurpose SOI for the catalysis of new-to-nature Fe-based chemical reactions. The high-resolution structures of SOI provide a foundation for further engineering and optimization of the enzyme for industrial biocatalysis and Meinwald rearrangements.

The enzyme has the potential to be extremely useful in the chemical and pharmaceutical industries, allowing for the production of precursors for drugs and important chemicals under energy-saving and environmentally friendly conditions. Its stability also makes it suitable for large-scale industrial applications. "It will certainly become a new, important tool for the circular economy and green chemistry," the PSI researchers stated.

Key Takeaways

  • Researchers reveal high-resolution structure of styrene oxide isomerase (SOI) enzyme.
  • SOI's unique catalytic mechanism and ferric haem b prosthetic group enable energy-saving production of drug precursors.
  • Enzyme's stability and specificity make it suitable for large-scale industrial applications.
  • SOI can catalyze Meinwald rearrangements, supporting green chemistry and circular economy.
  • Findings can lead to engineering and optimization of SOI for industrial biocatalysis.