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学者姓名：林娟
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Abstract ：
Ophiocordyceps sinensis fruit bodies, an insect-fungi complex, is a renowned ingredient in traditional Chinese medicine. Although numerous previous reviews have concentrated on the bioactive components and pharmacological properties of O. sinensis fruit bodies, there remains a notable lack of literature regarding the development of novel methods for authenticating these fruit bodies, particularly in the context of applying molecular identification techniques. The authentication of O. sinensis fruit bodies poses significant challenges due to the widespread contamination of these ingredients with counterfeit products. This article first provides an overview of the life cycle, biological characteristics, and habitat of O. sinensis. It then summarizes the importance of molecular identification techniques for O. sinensis and outlines the main techniques related to DNA molecular manipulation for the identification of medicinal plants, including Cordyceps and its related species. The article concludes by emphasizing the application of these identification techniques in the study of O. sinensis over the past decade. Additionally, the review suggests the potential of using molecular biology and multi-omics techniques to elucidate differences among biological individuals in complex environments and to construct microbial fingerprint maps for verifying the authenticity of Cordyceps and its related species. This review provides a scientific reference for the development of new detection methods for rapid and accurate authentication of O. sinensis and its related species.
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| GB/T 7714 | Yang, J. , Zhang, L. , Qun, P. et al. Molecular Identification Technologies in Authentication of Chinese Caterpillar Mushroom Ophiocordyceps sinensis (Ascomycota) and Related Species: A Review [J]. | International journal of medicinal mushrooms , 2025 , 27 (11) : 21-35 . |
| MLA | Yang, J. et al. "Molecular Identification Technologies in Authentication of Chinese Caterpillar Mushroom Ophiocordyceps sinensis (Ascomycota) and Related Species: A Review" . | International journal of medicinal mushrooms 27 . 11 (2025) : 21-35 . |
| APA | Yang, J. , Zhang, L. , Qun, P. , Lin, J. , Zhou, X. . Molecular Identification Technologies in Authentication of Chinese Caterpillar Mushroom Ophiocordyceps sinensis (Ascomycota) and Related Species: A Review . | International journal of medicinal mushrooms , 2025 , 27 (11) , 21-35 . |
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Chiral sulfinamides find broad applications in bioactive compounds, chiral auxiliaries, chiral ligands, and organocatalysts. However, biocatalytic approaches for their enantioselective synthesis have rarely been explored. Herein, an efficient biocatalytic strategy for the synthesis of chiral sulfinamides via polycyclic ketone monooxygenase (PockeMO) catalyzed asymmetric oxidation of sulfenamides was reported. A diverse array of chiral sulfinamides can be readily accessed with high yields (up to >99%) and enantioselectivities (>99:1 er). Additionally, this biocatalytic platform was scalable, and the resulting synthetic chiral sulfinamides could be easily derivatized to various chiral S-stereogenic compounds. Molecular dynamics simulation studies revealed that hydrogen bonding interactions between the sulfenamides and key residues were essential for enantioselectivity control. This work unlocks a biocatalytic avenue to access chiral sulfinamides for synthetic chemistry and drug discovery.
Keyword ：
asymmetric oxidation asymmetric oxidation biocatalysis biocatalysis chiralsulfinamides chiralsulfinamides polycyclic ketone monooxygenase (PockeMO) polycyclic ketone monooxygenase (PockeMO) sulfenamides sulfenamides
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| GB/T 7714 | Xue, Wanqing , Lin, Yuqi , Lin, Xiaomin et al. Synthesis of Chiral Sulfinamides Enabled by Polycyclic Ketone Monooxygenase Catalyzed Asymmetric Oxidation of Sulfenamides [J]. | ACS CATALYSIS , 2025 , 15 (18) : 16247-16253 . |
| MLA | Xue, Wanqing et al. "Synthesis of Chiral Sulfinamides Enabled by Polycyclic Ketone Monooxygenase Catalyzed Asymmetric Oxidation of Sulfenamides" . | ACS CATALYSIS 15 . 18 (2025) : 16247-16253 . |
| APA | Xue, Wanqing , Lin, Yuqi , Lin, Xiaomin , Xu, Xinqi , Chen, Jingjing , Lin, Juan et al. Synthesis of Chiral Sulfinamides Enabled by Polycyclic Ketone Monooxygenase Catalyzed Asymmetric Oxidation of Sulfenamides . | ACS CATALYSIS , 2025 , 15 (18) , 16247-16253 . |
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4-Acetoxy-azacyclobutanone (4AA) is a highly demanded chemical compound used in the production of Penem and Carbapenem antibiotics. However, its synthesis is constrained by the preparation of methyl (2S,3R)-2-[(benzoylamino)methyl]-3-hydroxybutanoate [(2S,3R)-BHME]. In light of stringent environmental regulations, there is an urgent need to develop an effective enzymatic method using 2-benzoylaminomethyl-3-oxy-butyrate methyl ester (BOME) as the substrate. This study mined a carbonyl reductase AxSDR from Algoriella xinjiangensis, which asymmetrically reduces BOME to (2S,3R)-BHME using isopropanol (IPA) as a cosubstrate. The mechanisms underlying the high stereoselectivity, substrate selectivity, and limited activity of AxSDR toward BOME were analyzed using computer-aided technology. Based on these analyses, AxSDR was rationally designed, leading to the identification of a triple-point variant, G94T/H145Y/Y188L (Mu3), which exhibited a 2-fold increase in catalytic efficiency. After condition optimization, Mu3 cells were able to convert 300 mM BOME, achieving a space-time yield of 15.1 g/L/h. The sustainability of the (2S,3R)-BHME biosynthesis method was further enhanced by immobilizing Mu3 on IPA-tolerant amino resin. The space-time yield of the immobilized enzyme Mu3-imm increased to 75.3 g/(Lh) and was maintained at 50.2 g/(Lh) after 100 uses. These results demonstrate the significant industrial application potential of Mu3-imm in reducing the costs and environmental risks associated with the preparation of (2S,3R)-BHME and its downstream products such as 4-AA, Penem, and Carbapenem antibiotics.
Keyword ：
asymmetrically reduction asymmetrically reduction carbonyl reductases carbonyl reductases immobilization immobilization methyl (2S,3R)-2-[(benzoylamino)methyl]-3-hydroxybutanoate methyl (2S,3R)-2-[(benzoylamino)methyl]-3-hydroxybutanoate rational design rational design sustainability sustainability
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| GB/T 7714 | Meng, Fengwei , Su, Bingmei , Lin, Juan . Biosynthesis of Methyl (2S,3R)-2-[(Benzoylamino)methyl]-3-hydroxybutanoate in High Space-Time Yield with Immobilized Engineered Carbonyl Reductase [J]. | ACS SUSTAINABLE CHEMISTRY & ENGINEERING , 2025 , 13 (2) : 767-777 . |
| MLA | Meng, Fengwei et al. "Biosynthesis of Methyl (2S,3R)-2-[(Benzoylamino)methyl]-3-hydroxybutanoate in High Space-Time Yield with Immobilized Engineered Carbonyl Reductase" . | ACS SUSTAINABLE CHEMISTRY & ENGINEERING 13 . 2 (2025) : 767-777 . |
| APA | Meng, Fengwei , Su, Bingmei , Lin, Juan . Biosynthesis of Methyl (2S,3R)-2-[(Benzoylamino)methyl]-3-hydroxybutanoate in High Space-Time Yield with Immobilized Engineered Carbonyl Reductase . | ACS SUSTAINABLE CHEMISTRY & ENGINEERING , 2025 , 13 (2) , 767-777 . |
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Baeyer-Villiger monooxygenases (BVMOs) can catalyze the asymmetric sulfoxidation to form pharmaceutical prazoles in environmentally friendly approach. In this work, the thermostable BVMO named PockeMO had high sulfoxidation activity towards rabeprazole sulfide to form (R)-rabeprazole but demonstrated significant overoxidation activity to form undesired sulfone by-product. To address this issue, the enzyme was engineered based on the computer assisted comparison for the substrate binding conformations. A mutant S482Y/L532Q (MU2) was obtained with much alleviated overoxidation activity and enhanced sulfoxidation activity towards rabeprazole sulfide. The catalytic efficiency for (R)-rabeprazole oxidation decreased 35 folds and increased 40 folds for the sulfoxidation of lansoprazole sulfide. The structural mechanism for the selectivity improvement was illuminated to find a selectivity decision pocket that was conservatively present in BVMOs composed of 4 loops. In upscaled reaction system, the substrate loading for MU2 increased from 40 mM to 100 mM for the synthesis of enantiopure (R)-rabeprazole. The sulfone content decreased from 16.6 % to 1.2 % compared to PockeMO. Lansoprazole sulfide could also be fully converted into enantiopure (R)-lansoprazole at 50 mM in 4 h by MU2 while PockeMO almost did not have activity. This work indicated the synthetic applicability of MU2 for active pharmaceutical (R)-prazoles.
Keyword ：
Baeyer-Villiger monooxygenase Baeyer-Villiger monooxygenase ( R )-prazole ( R )-prazole Substrate selectivity Substrate selectivity
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| GB/T 7714 | Xu, Xinqi , Xu, Fahui , Chen, Jingjing et al. Engineering of a (R)-selective Baeyer-Villiger monooxygenase to minimize overoxidation activity for asymmetric synthesis of active pharmaceutical prazoles [J]. | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES , 2025 , 296 . |
| MLA | Xu, Xinqi et al. "Engineering of a (R)-selective Baeyer-Villiger monooxygenase to minimize overoxidation activity for asymmetric synthesis of active pharmaceutical prazoles" . | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES 296 (2025) . |
| APA | Xu, Xinqi , Xu, Fahui , Chen, Jingjing , Wang, Shumin , Wang, Xialian , Su, Bingmei et al. Engineering of a (R)-selective Baeyer-Villiger monooxygenase to minimize overoxidation activity for asymmetric synthesis of active pharmaceutical prazoles . | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES , 2025 , 296 . |
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Hydroxytyrosol, a naturally occurring chemical with antioxidant and antiviral properties, is widely used in the nutrition, pharmaceutical, and cosmetic industries. In the present study, a modularized cascade composed of Modules 1 and 2 was designed and implemented to convert L-tyrosine to hydroxytyrosol. Module 1 was a fourenzymatic cascade for converting L-tyrosine to tyrosol. Engineering Module 1 by fine-tuning the expression of the desired enzymes resulted in a robust whole-cell catalyst, BL21 (M1-13), which converted L-tyrosine to tyrosol at high substrate loading. Module 2 involved a 4-hydroxyphenylacetate 3-monooxygenase (HpaBC)-catalyzed reaction to hydroxylate tyrosol to form hydroxytyrosol. The rational design of the HpaB subunit led to a positive variant, HpaB-Mu (T292S/R474A), which was subsequently applied to Module 2 for tyrosol hydroxylation, yielding a robust whole-cell catalyst, BL21 (M2-05). The two designed modules were merged for one-pot conversion of L-tyrosine to hydroxytyrosol by adjusting the ratio and total amount of whole-cell catalyst loading, capable of converting 40 mM of L-tyrosine to 35.8 mM of hydroxytyrosol with a high space-time yield (1.38 g/L/ h). The current study proved that engineering HpaB at the substrate tunnel was a feasible way to boost its activity and proposed an effective method for synthesizing hydroxytyrosol from low-cost substrates, which has great economic potential.
Keyword ：
Enzymatic cascade Enzymatic cascade HpaB HpaB Hydroxytyrosol Hydroxytyrosol Rational design Rational design
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| GB/T 7714 | Liu, Wen-Kai , Ren, Xiu-Xin , Xu, Lian et al. Modular cascade with engineered HpaB for efficient synthesis of hydroxytyrosol [J]. | BIOORGANIC CHEMISTRY , 2025 , 155 . |
| MLA | Liu, Wen-Kai et al. "Modular cascade with engineered HpaB for efficient synthesis of hydroxytyrosol" . | BIOORGANIC CHEMISTRY 155 (2025) . |
| APA | Liu, Wen-Kai , Ren, Xiu-Xin , Xu, Lian , Lin, Juan . Modular cascade with engineered HpaB for efficient synthesis of hydroxytyrosol . | BIOORGANIC CHEMISTRY , 2025 , 155 . |
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Whole-cell redox-neutral cascade reactions are promising for the sustainable synthesis of bulky lactones. In this study, the cyclohexanone monooxygenase from Acinetobacter sp. NCIMB 9871 (CHMOAc) was rationally designed based on enhancing product release and consensus sequence design to enhance the activity and stability of the enzyme. A four-point mutant MU4 (G14A/A43G/M400L/F432I) showed improved activity and stability for the oxidation of cyclohexanone to epsilon-caprolactone at a high substrate loading. A newly NADPH-dependent alcohol dehydrogenase from Pseudomonas monteilii (PmADH) with high cyclohexanol oxidation activity was introduced for constructing the redox-neutral cascade for the synthesis of epsilon-caprolactone from cyclohexanol. To improve the intracellular environment for cascade synthesis of epsilon-caprolactone, CRISPR/Cas9-mediated strong promoter insertion to the endogenous catalase gene katE in the NADP self-sufficient Escherichia coli strain BK-1 (Ptrc-nadK/Ptrc-pncB) was done for mitigating the oxidative stress to obtain the strain E. coli BKE-3 harboring MU4 and PmADH. Finally, 776 mM cyclohexanol could be converted into epsilon-caprolactone by the BKE-3 whole-cell catalytic system with a >99% conversion rate without cyclohexanone accumulation, which was the highest record for the redox-neutral cascade synthesis of epsilon-caprolactone. The BKE-3 whole-cell catalytic system also showed high efficiency for the synthesis of various lactones. This work provides an efficient redox-neutral catalytic platform for the sustainable synthesis of lactones featuring high substrate loading and atomic economy.
Keyword ：
CRISPR/Cas9genome editing CRISPR/Cas9genome editing cyclohexanone monooxygenase cyclohexanone monooxygenase enzymatic cascade enzymatic cascade epsilon-caprolactone epsilon-caprolactone protein engineering protein engineering
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| GB/T 7714 | Xu, Xinqi , Wang, Shumin , Zhong, Yaqun et al. Rational Design of Cyclohexanone Monooxygenase and a Whole-Cell System for Biocatalytic Redox-Neutral Cascade Synthesis of Lactones [J]. | ACS SUSTAINABLE CHEMISTRY & ENGINEERING , 2025 , 13 (33) : 13340-13353 . |
| MLA | Xu, Xinqi et al. "Rational Design of Cyclohexanone Monooxygenase and a Whole-Cell System for Biocatalytic Redox-Neutral Cascade Synthesis of Lactones" . | ACS SUSTAINABLE CHEMISTRY & ENGINEERING 13 . 33 (2025) : 13340-13353 . |
| APA | Xu, Xinqi , Wang, Shumin , Zhong, Yaqun , Yang, Juanjuan , Xu, Lian , Su, Bingmei et al. Rational Design of Cyclohexanone Monooxygenase and a Whole-Cell System for Biocatalytic Redox-Neutral Cascade Synthesis of Lactones . | ACS SUSTAINABLE CHEMISTRY & ENGINEERING , 2025 , 13 (33) , 13340-13353 . |
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5-Hydroxytryptophan (5-HTP) is widely used as a natural remedy for sleep disorders. In terms of biosafety, bio-derived 5-HTP is preferred over chemically synthesized 5-HTP. However, the low titer of 5-HTP in the reported microbiological methods (< 10 g/L) limits the industrialization of 5-HTP biosynthesis. In the present study, a Trp-accumulating E. coli strain TRP1 was constructed by blocking the degradation path (Delta tnaA), branching paths (Delta pheA, Delta tyrA) and repression system (Delta trpR, Delta trpL). Next, the hydroxylation module employing a phenylalanine hydroxylase mutant XcPAH(W179F) (XC2) coupled with an MH4 regenerating system (CvPCD-EcFolM system) was screened to convert L-Trp into 5-HTP. Protein engineering was performed on hydroxylase XC2 based on the molecular dynamics simulation of the enzyme-substrate complex, and the strain TRP1-XC4 harboring the triple-mutant XcPAH(L98I/A129K/W179F) (XC4) was able to produce 319.4 mg/L 5-HTP. Genome editing was carried out focused on accelerating product efflux (strengthening YddG) and increasing MH4 supply (strengthening FolM, FolE and FolX), resulting in a strain TRP5-XC4 to produce 13.9 g/L 5-HTP in 5 L fed-batch fermentation with a space-time yield of 0.29 g/L/h, which is the highest production and productivity record for 5-HTP biosynthesis. This study successfully provided an engineered strain and an efficient green method for the industrial synthesis of 5-HTP. [GRAPHICS] .
Keyword ：
5-Hydroxytryptophan 5-Hydroxytryptophan Cofactor engineering Cofactor engineering Genome editing Genome editing Phenylalanine hydroxylase Phenylalanine hydroxylase Protein engineering Protein engineering
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| GB/T 7714 | Ai, Yulin , Huang, Yusong , Zhao, Hongru et al. Engineered phenylalanine hydroxylase coupled with an effective cofactor synthesis and regeneration system for high-yield production of 5-hydroxytryptophan [J]. | BIORESOURCES AND BIOPROCESSING , 2025 , 12 (1) . |
| MLA | Ai, Yulin et al. "Engineered phenylalanine hydroxylase coupled with an effective cofactor synthesis and regeneration system for high-yield production of 5-hydroxytryptophan" . | BIORESOURCES AND BIOPROCESSING 12 . 1 (2025) . |
| APA | Ai, Yulin , Huang, Yusong , Zhao, Hongru , Su, Bingmei , Lin, Juan . Engineered phenylalanine hydroxylase coupled with an effective cofactor synthesis and regeneration system for high-yield production of 5-hydroxytryptophan . | BIORESOURCES AND BIOPROCESSING , 2025 , 12 (1) . |
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Hydroxytyrosol, a naturally occurring compound with antioxidant and antiviral activity, is widely applied in the cosmetic, food, and nutraceutical industries. The development of a biocatalytic approach for producing hydroxytyrosol from simple and readily accessible substrates remains a challenge. Here, we designed and implemented an effective biocatalytic cascade to obtain hydroxytyrosol from 3,4-dihydroxybenzaldehyde and l-threonine via a four-step enzymatic cascade composed of seven enzymes. To prevent cross-reactions and protein expression burden caused by multiple enzymes expressed in a single cell, the designed enzymatic cascade was divided into two modules and catalyzed in a stepwise manner. The first module (FM) assisted the assembly of 3,4-dihydroxybenzaldehyde and l-threonine into (2S,3R)-2-amino-3-(3,4-dihydroxyphenyl)-3-hydroxypropanoic acid, and the second module (SM) entailed converting (2S,3R)-2-amino-3-(3,4-dihydroxyphenyl)-3-hydroxypropanoic acid into hydroxytyrosol. Each module was cloned into Escherichia coli BL21 (DE3) and engineered in parallel by fine-tuning enzyme expression, resulting in two engineered whole-cell catalyst modules, BL21(FM01) and BL21(SM13), capable of converting 30 mM 3,4-dihydroxybenzaldehyde to 28.7 mM hydroxytyrosol with a high space-time yield (0.88 g/L/h). To summarize, the current study proposes a simple and effective approach for biosynthesizing hydroxytyrosol from low-cost substrates and thus has great potential for industrial applications.
Keyword ：
Biocatalytic cascade Biocatalytic cascade hydroxytyrosol hydroxytyrosol stepwisecatalysis stepwisecatalysis
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| GB/T 7714 | Liu, Wen-Kai , Su, Bing-Mei , Xu, Xin-Qi et al. Multienzymatic Cascade for Synthesis of Hydroxytyrosol via Two-Stage Biocatalysis [J]. | JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY , 2024 , 72 (27) : 15293-15300 . |
| MLA | Liu, Wen-Kai et al. "Multienzymatic Cascade for Synthesis of Hydroxytyrosol via Two-Stage Biocatalysis" . | JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY 72 . 27 (2024) : 15293-15300 . |
| APA | Liu, Wen-Kai , Su, Bing-Mei , Xu, Xin-Qi , Xu, Lian , Lin, Juan . Multienzymatic Cascade for Synthesis of Hydroxytyrosol via Two-Stage Biocatalysis . | JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY , 2024 , 72 (27) , 15293-15300 . |
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Norepinephrine, a kind of beta-adrenergic receptor agonist, is commonly used for treating shocks and hypotension caused by a variety of symptoms. The development of a straightforward, efficient and environmentally friendly biocatalytic route for manufacturing norepinephrine remains a challenge. Here, we designed and realized an artificial biocatalytic cascade to access norepinephrine starting from 3, 4-dihydroxybenzaldehyde and L-threonine mediated by a tailored-made L-threonine transaldolase PsLTTA-Mu1 and a newly screened tyrosine decarboxylase ErTDC. To overcome the imbalance of multi-enzymes in a single cell, engineering of PsLTTA for improved activity and fine-tuning expression mode of multi-enzymes in single E.coli cells were combined, leading to a robust whole cell biocatalyst ES07 that could produce 100 mM norepinephrine with 99% conversion, delivering a highest time-space yield (3.38 g/L/h) ever reported. To summarized, the current study proposed an effective biocatalytic approach for the synthesis of norepinephrine from low-cost substrates, paving the way for industrial applications of enzymatic norepinephrine production.
Keyword ：
Biocatalytic cascade Biocatalytic cascade L-threonine transaldolase L-threonine transaldolase Tyrosine decarboxylase Tyrosine decarboxylase
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| GB/T 7714 | Xu, Lian , Shen, Jun-Jiang , Wu, Ming et al. An artificial biocatalytic cascade for efficient synthesis of norepinephrine by combination of engineered L-threonine transaldolase with multi-enzyme expression fine-tuning [J]. | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES , 2024 , 265 . |
| MLA | Xu, Lian et al. "An artificial biocatalytic cascade for efficient synthesis of norepinephrine by combination of engineered L-threonine transaldolase with multi-enzyme expression fine-tuning" . | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES 265 (2024) . |
| APA | Xu, Lian , Shen, Jun-Jiang , Wu, Ming , Su, Bing-Mei , Xu, Xin-Qi , Lin, Juan . An artificial biocatalytic cascade for efficient synthesis of norepinephrine by combination of engineered L-threonine transaldolase with multi-enzyme expression fine-tuning . | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES , 2024 , 265 . |
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Organofluorine compounds find extensive application in the fields of agrochemicals, pharmaceuticals, materials science, and molecular imaging. Introducing fluorine atoms can provide organic compounds with unique physicochemical properties or improve their biological activity. Although significant progress has been made in the chemical synthesis of fluorine-containing compounds, achieving selective fluorination under mild conditions remains extremely challenging. Introducing biocatalytic approaches in organofluorine chemistry is an important strategy given their high efficiency, selectivity, and environmental friendliness. In this review, we present the discovery of fluorinated natural products and fluorinases, the crystal structure and the directed evolution of fluorinases, with a focus on recent advances in the enzymatic synthesis of fluorine-containing compounds in recent years. It is hoped that this review will help to promote the field of biocatalytic organofluorine compound synthesis. Organofluorine compounds play a crucial role in agrochemicals, pharmaceuticals, and materials science. Biocatalysis has emerged as an essential strategy in the synthesis of fluorinated molecules under mild conditions. This review mainly focused on recent advances in the enzymatic synthesis of fluorine-containing compounds. Furthermore, the identification of fluorinated natural products and fluorinases, the crystal structure and the directed evolution of fluorinases were discussed. image
Keyword ：
C-F bond C-F bond enzyme enzyme fluorinase fluorinase fluorinated compounds fluorinated compounds fluorination fluorination
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| GB/T 7714 | Lin, Yuqi , Xue, Wanqing , Li, Hechen et al. Advances in Enzymatic Incorporation of Small Fluorine Modules [J]. | EUROPEAN JOURNAL OF ORGANIC CHEMISTRY , 2024 , 27 (17) . |
| MLA | Lin, Yuqi et al. "Advances in Enzymatic Incorporation of Small Fluorine Modules" . | EUROPEAN JOURNAL OF ORGANIC CHEMISTRY 27 . 17 (2024) . |
| APA | Lin, Yuqi , Xue, Wanqing , Li, Hechen , Su, Bingmei , Lin, Juan , Ye, Ke-Yin . Advances in Enzymatic Incorporation of Small Fluorine Modules . | EUROPEAN JOURNAL OF ORGANIC CHEMISTRY , 2024 , 27 (17) . |
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