Light has received increased attention for various chemical reactions but also in combination with biocatalytic reactions. Because currently only a few enzymatic reactions are known, which per se ...require light, most transformations involving light and a biocatalyst exploit light either for providing the cosubstrate or cofactor in an appropriate redox state for the biotransformation. In selected cases, a promiscuous activity of known enzymes in the presence of light could be induced. In other approaches, light-induced chemical reactions have been combined with a biocatalytic step, or light-induced biocatalytic reactions were combined with chemical reactions in a linear cascade. Finally, enzymes with a light switchable moiety have been investigated to turn off/on or tune the actual reaction. This Review gives an overview of the various approaches for using light in biocatalysis.
S‐adenosylmethionine‐dependent methyltransferases are involved in countless biological processes, including signal transduction, epigenetics, natural product biosynthesis, and detoxification. Only a ...handful of carboxylate methyltransferases have evolved to participate in amide bond formation. In this report we show that enzyme‐catalyzed F‐methylation of carboxylate substrates produces F‐methyl esters that readily react with N‐ or S‐nucleophiles under physiological conditions. We demonstrate the applicability of this approach to the synthesis of small amides, hydroxamates, and thioesters, as well as to site‐specific protein modification and native chemical ligation.
This report shows that methyltransferase‐mediated fluoromethylation can activate small and large carboxylate substrates for conjugation to thiols, hydrazine, hydroxylamine or amines. This methodology to produce anhydrides offers an alternative to the much more common ATP‐dependent processes observed in nature and utilized in biocatalysis.
Biocatalysis within biphasic systems is gaining significant attention in the field of synthetic chemistry, primarily for its ability to solve the problem of incompatible solubilities between ...biocatalysts and organic compounds. By forming an emulsion from these two-phase systems, a larger surface area is created, which greatly improves the mass transfer of substrates to the biocatalysts. Among the various types of emulsions, Pickering emulsions stand out due to their excellent stability, compatibility with biological substances, and the ease with which they can be formed and separated. This makes them ideal for reusing both the emulsifiers and the biocatalysts. This review explores the latest developments in biocatalysis using Pickering emulsions. It covers the structural features, methods of creation, innovations in flow biocatalysis, and the role of interfaces in these processes. Additionally, the challenges and future directions are discussed in combining chemical and biological catalysts within Pickering emulsion frameworks to advance synthetic methodologies.
•MOFs with different dimensionalities are a versatile host platform for the effective enzymes immobilization.•Dimensionality of MOFs significantly affects performance of enzyme@MOF ...composites.•Preparation approaches of enzyme@MOF composites with different dimensionalities are evaluated.•There will be great demand on enzyme@MOF composites with diverse functionality.
Metal-organic frameworks (MOFs) are an emerging class of porous materials with well-defined pore and crystal structure, favorable biocompatibility, good chemo-/machinal stability and high surface area, which endow them as ideal host matrix to develop enzyme@MOF composites. Most of the enzyme@MOF composites exhibit excellent catalysis performances performance and increased stability. In the past decade, many efforts have been made to develop enzyme@MOF composites with potential applications. The dimensionality of the MOFs has a significant effect on the catalytic performance of enzyme@MOF composites. However, there have been few reviews on enzyme@MOF composites with different dimensionalities. This review aims to describe the contemporary advances in the development of enzyme@MOF composites with different dimensionalities. Synthesizing strategies of enzyme@MOF composites with different dimensionalities are summarized. The interaction between enzymes and MOFs with different dimensionalities from the aspects of activity, stability, and reusability are discussed. Furthermore, the application and potential research direction of enzyme@MOF composites are introduced. We believe this work will be helpful for readers to understand the fundamental research and applications of enzyme@MOF composites with different dimensionalities.
Ionic liquids have unique chemical properties that have fascinated scientists in many fields. The effects of adding ionic liquids to biocatalysts are many and varied. The uses of ionic liquids in ...biocatalysis include improved separations and phase behaviour, reduction in toxicity, and stabilization of protein structures. As the ionic liquid state of the art has progressed, concepts of what can be achieved in biocatalysis using ionic liquids have evolved and more beneficial effects have been discovered. In this review ionic liquids for whole-cell and isolated enzyme biocatalysis will be discussed with an emphasis on the latest developments, and a look to the future.
Vinyl and p‐nitrophenyl esters have emerged as alternative substrates for the LovD9 acylation mechanism, showing product yields as high as those obtained by ...α‐dimethylbutyryl‐S‐methyl‐3‐mercaptopropionate (DMB‐SMMP), the thioester for which LovD9 was evolved. More information can be found in the Research Article by G. Jiménez‐Osés, F. López‐Gallego and co‐workers (DOI: 10.1002/chem.202300911).
A chemoenzymatic cascade process for the sustainable production of pyrroles has been developed. Pyrroles were synthesized by exploiting the previously unexplored aromatizing activity of monoamine ...oxidase enzymes (MAO-N and 6-HDNO). MAO-N/6-HDNO whole cell biocatalysts are able to convert 3-pyrrolines into pyrroles under mild conditions and in high yields. Moreover, MAO-N can work in combination with the ruthenium Grubbs catalyst, leading to the synthesis of pyrroles from diallylamines/-anilines in a one-pot cascade metathesis–aromatization sequence.
Enzymatic carbon dioxide fixation is one of the most important metabolic reactions as it allows the capture of inorganic carbon from the atmosphere and its conversion into organic biomass. However, ...due to the often unfavorable thermodynamics and the difficulties associated with the utilization of CO
, a gaseous substrate that is found in comparatively low concentrations in the atmosphere, such reactions remain challenging for biotechnological applications. Nature has tackled these problems by evolution of dedicated CO
-fixing enzymes, i.e., carboxylases, and embedding them in complex metabolic pathways. Biotechnology employs such carboxylating and decarboxylating enzymes for the carboxylation of aromatic and aliphatic substrates either by embedding them into more complex reaction cascades or by shifting the reaction equilibrium via reaction engineering. This review aims to provide an overview of natural CO
-fixing enzymes and their mechanistic similarities. We also discuss biocatalytic applications of carboxylases and decarboxylases for the synthesis of valuable products and provide a separate summary of strategies to improve the efficiency of such processes. We briefly summarize natural CO
fixation pathways, provide a roadmap for the design and implementation of artificial carbon fixation pathways, and highlight examples of biocatalytic cascades involving carboxylases. Additionally, we suggest that biochemical utilization of reduced CO
derivates, such as formate or methanol, represents a suitable alternative to direct use of CO
and provide several examples. Our discussion closes with a techno-economic perspective on enzymatic CO
fixation and its potential to reduce CO
emissions.
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