Chemoenzymatic synthesis

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Nature has been a source of constant inspiration for chemists, not only because of the enormous variety of chemical compounds that living organisms can produce, but also because of the extraordinary biosynthetic strategies used to obtain them.

Leveraging the power of nature for sustainable chemical synthesis, utilizing enzymes as biocatalysts in chemical reactions can significantly accelerate product formation under mild reaction conditions (i.e. ambient temperature and pressure, neutral pH, etc.) and transform organic substrates with excellent chemo-, regio-, and stereoselectivity while preserving the requirements of environmental benignity. Therefore, enzymes have become an important tool for preparing chiral molecules in a highly efficient, straightforward, and selective fashion, often drastically outperforming the catalytic potential of synthetic transition-metal catalysts and organocatalysts.

Moreover, incorporating enzymes into chemical technologies can dramatically shorten the synthetic pathways, leading to less toxic waste generation and improved cost-efficiency. In this context, recent years have seen significant efforts in mimicking the metabolism of living organisms by combining several types of enzymes in a single reaction vessel to obtain complex molecules without isolating intermediates. Such artificial 'one-pot' biocatalytic cascade reactions have opened new avenues for challenging synthetic endeavors, especially for manufacturing chiral drugs, in which the chemical and optical purity of active pharmaceutical ingredients are paramount factors for therapeutic activity and safety of usage.

This Collection aims to present the latest progress in the chemoenzymatic syntheses of high-value-added organic compounds, which can be utilized in the production of drugs, agrochemicals, flavors and fragrances, food additives, cosmetics, natural products, etc. We also intend for the Collection to highlight ongoing challenges and opportunities in developing new biocatalysts or chemoenzymatic strategies, exploring new catalytic reactions, and supporting cutting-edge technologies that enable functional materials and biofuel production. In this context, we welcome both experimental and theoretical studies, with topics of interest including but not limited to:

  • Enzyme engineering
  • Multienzymatic cascades
  • Chemoenzymatic cascades
  • Metalloenzymes
  • Photo-biocatalysis
  • Multifunctional biocatalysts
  • Enzyme promiscuity

The Collection primarily welcomes original research papers in the form of both full articles and communications. All submissions will be subject to the same review process and editorial standards as regular Communications Chemistry Articles.

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The crystal structure of alcohol dehydrogenase bound to NADP cofactor from Lactobacillus kefir


Dr. Jennifer Bridwell-Rabb is an Assistant Professor in the Department of Chemistry at the University of Michigan, Ann Arbor. Her research group studies the oxygen-dependent and oxygen-independent mechanisms of enzymes that catalyze a wide-range of site-specific chemistry using enzymology, structural biology, and metalloprotein expertise. Her laboratory is particularly interested in the transformations catalyzed by the Rieske non-heme oxygenase enzymes, the metalloprotein chemistry required to build, modify, and degrade photosynthetic pigments, and the strategies that photosynthetic organisms use to adapt to environments that differ in oxygen- and light-availability.

Dr. Paweł Borowiecki is an Assistant Professor in the Chair of Drug and Cosmetics Biotechnology at the Faculty of Chemistry, Warsaw University of Technology (WUT). He received his Ph.D. degree (2016) in Biotechnology from the Warsaw University of Technology. In 2020 he became a Head of the Laboratory of Biocatalysis and Biotransformation at WUT. His favorite research field encompasses developing novel chemoenzymatic strategies in the asymmetric synthesis of non-racemic pharmaceuticals and biologically active compounds potentially valuable for treating various life-threatening diseases.

Dr. Sandy Schmidt is a tenure-track assistant professor (Rosalind Franklin Fellow) at the Groningen Research Institute of Pharmacy, University of Groningen. She completed her Ph.D. at the University of Greifswald in 2015, followed by a research stay at Delft University of Technology as a postdoctoral fellow. From 2017-2020, she worked as a group leader at Graz University of Technology. Her research interests include the discovery, design and exploitation of novel iron-dependent biocatalysts and the development of photobiocatalytic approaches for applications in organic synthesis.