Regioselectivity-Switchable Catalytic Annulations of Alkynyl α-Diketones and α-Cyanoketones.

07:00 EST 3rd December 2019 | BioPortfolio

Summary of "Regioselectivity-Switchable Catalytic Annulations of Alkynyl α-Diketones and α-Cyanoketones."

Regioselectivity-switchable reactions hold irreplaceable importance in the construction of diversified architectures. In this work, Brønsted base-catalyzed regioselectivity-switchable annulations between alkynyl α-diketones and α-cyanoketones have been achieved for the first time, delivering a series of skeletally thoroughly different dihydrofurofuran and furan derivatives. A range of novel transformations of the products can be realized. The work also demonstrates the unique features of alkynyl α-diketone chemistry, which are in sharp contrast to the current understanding of ynone-related chemistry.


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This article was published in the following journal.

Name: Organic letters
ISSN: 1523-7052


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Medical and Biotech [MESH] Definitions

RNA that has catalytic activity. The catalytic RNA sequence folds to form a complex surface that can function as an enzyme in reactions with itself and other molecules. It may function even in the absence of protein. There are numerous examples of RNA species that are acted upon by catalytic RNA, however the scope of this enzyme class is not limited to a particular type of substrate.

Biological molecules that possess catalytic activity. They may occur naturally or be synthetically created. Enzymes are usually proteins, however CATALYTIC RNA and CATALYTIC DNA molecules have also been identified.

Specific enzyme subunits that form the active sites of the type I and type II cyclic-AMP protein kinases. Each molecule of enzyme contains two catalytic subunits.

A phosphoprotein phosphatase subtype that is comprised of a catalytic subunit and two different regulatory subunits. At least two genes encode isoforms of the protein phosphatase catalytic subunit, while several isoforms of regulatory subunits exist due to the presence of multiple genes and the alternative splicing of their mRNAs. Protein phosphatase 2 acts on a broad variety of cellular proteins and may play a role as a regulator of intracellular signaling processes.

A eukayrotic protein serine-threonine phosphatase subtype that dephosphorylates a wide variety of cellular proteins. The enzyme is comprised of a catalytic subunit and regulatory subunit. Several isoforms of the protein phosphatase catalytic subunit exist due to the presence of multiple genes and the alternative splicing of their mRNAs. A large number of proteins have been shown to act as regulatory subunits for this enzyme. Many of the regulatory subunits have additional cellular functions.

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