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Deacylative Thiolation by Redox-Neutral Aromatization-Driven C-C Fragmentation of Ketones.

ABSTRACT: Herein we report the development of deacylative thiolation of diverse methyl ketones. The reaction is redox-neutral, and heavy-metal-free, which provides a new way to introduce thioether groups site-specifically to unactivated aliphatic positions. It also features excellent functional group tolerance and broad substrate scope, thus allowing late-stage derivatization. The process benefits from efficient condensation between the activation reagent and ketone substrates, which triggers aromatization-driven C-C fragmentation and rapid radical coupling with thiosulfonates. Experimental and computational mechanistic studies suggest the involvement of a radical chain pathway.

SUBMITTER: Zhou X

PROVIDER: S-EPMC10240504 | biostudies-literature | 2023 Apr

REPOSITORIES: biostudies-literature

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Deacylative Thiolation by Redox-Neutral Aromatization-Driven C-C Fragmentation of Ketones.

Zhou Xukai X Pyle Daniel D Zhang Zining Z Dong Guangbin G

Angewandte Chemie (International ed. in English) 20230303 15

Herein we report the development of deacylative thiolation of diverse methyl ketones. The reaction is redox-neutral, and heavy-metal-free, which provides a new way to introduce thioether groups site-specifically to unactivated aliphatic positions. It also features excellent functional group tolerance and broad substrate scope, thus allowing late-stage derivatization. The process benefits from efficient condensation between the activation reagent and ketone substrates, which triggers aromatizatio ...[more]

PMID: 36800315

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Project description:Low molecular weight (LMW) thiols play an important role as thiol-cofactors for many enzymes and are crucial to maintain the reduced state of the cytoplasm. Most Gram-negative bacteria utilize glutathione (GSH) as major LMW thiol. However, in Gram-positive Actinomycetes and Firmicutes alternative LMW thiols, such as mycothiol (MSH) and bacillithiol (BSH) play related roles as GSH surrogates, respectively. Under conditions of hypochlorite stress, MSH and BSH are known to form mixed disulfides with protein thiols, termed as S-mycothiolation or S-bacillithiolation that function in thiol-protection and redox regulation. Protein S-thiolations are widespread redox-modifications discovered in different Gram-positive bacteria, such as Bacillus and Staphylococcus species, Mycobacterium smegmatis, Corynebacterium glutamicum and Corynebacterium diphtheriae. S-thiolated proteins are mainly involved in cellular metabolism, protein translation, redox regulation and antioxidant functions with some conserved targets across bacteria. The reduction of protein S-mycothiolations and S-bacillithiolations requires glutaredoxin-related mycoredoxin and bacilliredoxin pathways to regenerate protein functions. In this review, we present an overview of the functions of mycothiol and bacillithiol and their physiological roles in protein S-bacillithiolations and S-mycothiolations in Gram-positive bacteria. Significant progress has been made to characterize the role of protein S-thiolation in redox-regulation and thiol protection of main metabolic and antioxidant enzymes. However, the physiological roles of the pathways for regeneration are only beginning to emerge as well as their interactions with other cellular redox systems. Future studies should be also directed to explore the roles of protein S-thiolations and their redox pathways in pathogenic bacteria under infection conditions to discover new drug targets and treatment options against multiple antibiotic resistant bacteria.

Dataset Information

Deacylative Thiolation by Redox-Neutral Aromatization-Driven C-C Fragmentation of Ketones.

Publications

Deacylative Thiolation by Redox-Neutral Aromatization-Driven C-C Fragmentation of Ketones.

Similar Datasets

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