New Method for Preparation of Coumarins and Quinolinones via Pd-Catalyzed Intramolecular Hydroarylation of C−C Triple Bonds

Jia, Chengguo; Piao, Dongguo; Kitamura, Tsugio; Fujiwara, Yoshiyuki

doi:10.1021/jo000861q

Cited by 242 publications

(108 citation statements)

References 47 publications

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“…The crude products obtained with the recombinant E. coli strain from phenanthrene, naphthalene, 1-methylnaphthalene, 2-methylnaphthlene, dibenzofuran, dibenzothiophene, biphenyl, and diphenylmethane were determined by HPLC and thin-layer chromatography, and the products detected were purified by silica gel column chromatography. Table 2 shows the hydroxylated products which were identified by comparison with the previously reported spectral data (mass spectrometry and nuclear magnetic resonance data) (5,22,23,38,39,40,48), whose chemical structures are shown in Fig. 4.…”

Section: Downloaded Frommentioning

confidence: 95%

Molecular Characterization and Substrate Preference of a Polycyclic Aromatic Hydrocarbon Dioxygenase from Cycloclasticus sp. Strain A5

Kasai

Shindo

Harayama

et al. 2003

Appl Environ Microbiol

100

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Cycloclasticus sp. strain A5 is able to grow with petroleum polycyclic aromatic hydrocarbons (PAHs), including unsubstituted and substituted naphthalenes, dibenzothiophenes, phenanthrenes, and fluorenes. A set of genes responsible for the degradation of petroleum PAHs was isolated by using the ability of the organism to oxidize indole to indigo. This 10.5-kb DNA fragment was sequenced and found to contain 10 open reading frames (ORFs). Seven ORFs showed homology to previously characterized genes for PAH degradation and were designated phn genes, although the sequence and order of these phn genes were significantly different from the sequence and order of the known PAH-degrading genes. The phnA1, phnA2, phnA3, and phnA4 genes, which encode the ␣ and ␤ subunits of an iron-sulfur protein, a ferredoxin, and a ferredoxin reductase, respectively, were identified as the genes coding for PAH dioxygenase. The phnA4A3 gene cluster was located 3.7 kb downstream of the phnA2 gene. PhnA1 and PhnA2 exhibited moderate (less than 62%) sequence identity to the ␣ and ␤ subunits of other aromatic ring-hydroxylating dioxygenases, but motifs such as the Fe(II)-binding site and the [2Fe-2S] cluster ligands were conserved. Escherichia coli cells possessing the phnA1A2A3A4 genes were able to convert phenanthrene, naphthalene, and methylnaphthalene in addition to the tricyclic heterocycles dibenzofuran and dibenzothiophene to their hydroxylated forms. Significantly, the E. coli cells also transformed biphenyl and diphenylmethane, which are ordinarily the substrates of biphenyl dioxygenases.

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Section: Downloaded Frommentioning

confidence: 95%

Molecular Characterization and Substrate Preference of a Polycyclic Aromatic Hydrocarbon Dioxygenase from Cycloclasticus sp. Strain A5

Kasai

Shindo

Harayama

et al. 2003

Appl Environ Microbiol

100

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“…S1). Subsequent chemical optimization and the synthesis of over 40 substituted coumarin analogs of the initial screening hits led to the development of a panel of compounds with increased potency (17)(18)(19) (SI Appendix, Fig. S2).…”

Section: Identification Of a Series Of Substituted Coumarin Inhibitormentioning

confidence: 99%

Diarylcoumarins inhibit mycolic acid biosynthesis and kill Mycobacterium tuberculosis by targeting FadD32

Stanley

Kawate

Iwase

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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Infection with the bacterial pathogen Mycobacterium tuberculosis imposes an enormous burden on global public health. New antibiotics are urgently needed to combat the global tuberculosis pandemic; however, the development of new small molecules is hindered by a lack of validated drug targets. Here, we describe the identification of a 4,6-diaryl-5,7-dimethyl coumarin series that kills M. tuberculosis by inhibiting fatty acid degradation protein D32 (FadD32), an enzyme that is required for biosynthesis of cell-wall mycolic acids. These substituted coumarin inhibitors directly inhibit the acyl-acyl carrier protein synthetase activity of FadD32. They effectively block bacterial replication both in vitro and in animal models of tuberculosis, validating FadD32 as a target for antibiotic development that works in the same pathway as the established antibiotic isoniazid. Targeting new steps in well-validated biosynthetic pathways in antitubercular therapy is a powerful strategy that removes much of the usual uncertainty surrounding new targets and in vivo clinical efficacy, while circumventing existing resistance to established targets.

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“…[15] Recently, Pd-catalyzed coumarin syntheses presented a new promising strategy. [16] In 2006, Rao and Sivakumar reported a route to the synthesis of 3-aroylcoumarins by the condensation of a-aroylketene S,S-acetals and salicylaldehydes in the presence of catalytic amount of piperidine at reflux temperature.…”

mentioning

confidence: 99%

Copper(II)‐Catalyzed CC Bond‐Forming Reactions of α‐Electron‐Withdrawing Group‐Substituted Ketene S,S‐Acetals with Carbonyl Compounds and a Facile Synthesis of Coumarins

et al. 2009

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Abstract:A new catalytic C À C bond-forming reaction has been developed. Catalyzed by cheap and commercially available copper(II) bromide (CuBr 2 ; 10 mol%), the reactions of a-electron-withdrawing group (EWG)-substituted ketene S,S-acetals with aldehydes or ketones in acetonitrile at room temperature gave a variety of densely functionalized coupling products in excellent yields (80-98%). Based on this catalytic process, coumarin derivatives were efficiently synthesized when salicylaldehydes were selected as the carbonyl components.

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New Method for Preparation of Coumarins and Quinolinones via Pd-Catalyzed Intramolecular Hydroarylation of C−C Triple Bonds

Cited by 242 publications

References 47 publications

Molecular Characterization and Substrate Preference of a Polycyclic Aromatic Hydrocarbon Dioxygenase from Cycloclasticus sp. Strain A5

Molecular Characterization and Substrate Preference of a Polycyclic Aromatic Hydrocarbon Dioxygenase from Cycloclasticus sp. Strain A5

Diarylcoumarins inhibit mycolic acid biosynthesis and kill Mycobacterium tuberculosis by targeting FadD32

Copper(II)‐Catalyzed CC Bond‐Forming Reactions of α‐Electron‐Withdrawing Group‐Substituted Ketene S,S‐Acetals with Carbonyl Compounds and a Facile Synthesis of Coumarins

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