This study reports a strategy involving biocatalysis to form 2-alkylbenzoxazoles and 2-arylbenzoxazoles specifically via the urease-artificial Vitreoscilla hemoglobin metalloenzyme (ArVHbM)-catalyzed cascade reaction of urea, catechols, and aldehydes. In this system,...

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Organophosphorus compounds are the core structure of many active natural products. The synthesis of these compounds is generally achieved by metal catalysis requiring specifically functionalized substrates or harsh conditions. Herein, we disclose the phospha-Michael addition reaction of biphenyphosphine oxide with various substituted β-nitrostyrenes or benzylidene malononitriles. This biocatalytic strategy provides a direct route for the synthesis of C-P bonds with good functional group compatibility and simple and practical operation. Under the optimal conditions (styrene (0.5 mmol), biphenyphosphine oxide (0.5 mmol), Novozym 435 (300 U), and EtOH (1 mL)), lipase leads to the formation of organophosphorus compounds in yields up to 94% at room temperature. Furthermore, we confirm the role of the catalytic triad of lipase in this phospha-Michael addition reaction. This new biocatalytic system will have broad applications in organic synthesis.

A photocatalyzed, efficient, and mild approach for the synthesis of various substituted isothiocyanates from amine and carbon disulfide was reported in this work. This approach expands the scope of photocatalytic applications and provides a new method for the preparation of aliphatic and aromatic isothiocyanates, which are significant organic building blocks and biological diagnostic markers.

A metal‐free, straightforward, non‐hazardous reagent‐added, one‐pot approach for the efficient synthesis of 2‐arylimino‐2H‐chromenes with high yields was developed for the first time in this report through the coupling of salicylaldehydes with β‐ketothioamides, which was catalyzed by lipase in water. This green strategy provides an efficient method to obtain various 2‐arylimino‐2H‐chromenes and enriches the practical application of biocatalysis.