2017
Applications of Nonenzymatic Catalysts to the Alteration of Natural Products
Shugrue CR, Miller SJ. Applications of Nonenzymatic Catalysts to the Alteration of Natural Products. Chemical Reviews 2017, 117: 11894-11951. PMID: 28580785, PMCID: PMC5742423, DOI: 10.1021/acs.chemrev.7b00022.Peer-Reviewed Original ResearchConceptsNatural productsNonenzymatic catalystsComplex molecular scaffoldsComplex natural productsH bond functionalizationC bond formationNatural product scaffoldsLate-stage functionalizationNatural product derivativesSynthesis of analoguesChemical functionalityMedicinal chemistryBond functionalizationElectrophilic reagentsOlefin functionalizationSelectivity challengesBiological activity assaysBond formationEnzymatic catalystsProduct derivativesMolecular scaffoldsCatalystComplex moleculesChemical remodelingSmall molecules
2012
Mechanism of the Rhodium(III)-Catalyzed Arylation of Imines via C–H Bond Functionalization: Inhibition by Substrate
Tauchert ME, Incarvito CD, Rheingold AL, Bergman RG, Ellman JA. Mechanism of the Rhodium(III)-Catalyzed Arylation of Imines via C–H Bond Functionalization: Inhibition by Substrate. Journal Of The American Chemical Society 2012, 134: 1482-1485. PMID: 22257031, PMCID: PMC3269099, DOI: 10.1021/ja211110h.Peer-Reviewed Original ResearchConceptsCatalyzed ArylationH bond functionalizationC bond formationInverse first orderDetailed mechanistic studiesBond functionalizationStoichiometric reactionBond formationNew reactionFunctional groupsMechanistic studiesIminesArylationReactionFirst orderRelevant substratesSubstrateFunctionalizationCatalystAminesReactivityComplexes
2011
Linear and cyclic C -glycosides as surfactants
Foley P, Phimphachanh A, Beach E, Zimmerman J, Anastas P. Linear and cyclic C -glycosides as surfactants. Green Chemistry 2011, 13: 321-325. DOI: 10.1039/c0gc00407c.Peer-Reviewed Original ResearchCarbohydrate-based surfactantsAlkyl aldehydesC bond formationGlycosidic linkagesFacile synthesisBond formationReaction conditionsSurfactant propertiesGood yieldsSurfactantsAdditional analoguesRenewable feedstockC-glycosidesCarbohydrate CAldehydesMost carbohydratesNew classDesirable performance propertiesPerformance propertiesChemistryPyrrolidineRecent advancesPropertiesSynthesisStoichiometry
2010
Structure and function of an iterative polyketide synthase thioesterase domain catalyzing Claisen cyclization in aflatoxin biosynthesis
Korman TP, Crawford JM, Labonte JW, Newman AG, Wong J, Townsend CA, Tsai SC. Structure and function of an iterative polyketide synthase thioesterase domain catalyzing Claisen cyclization in aflatoxin biosynthesis. Proceedings Of The National Academy Of Sciences Of The United States Of America 2010, 107: 6246-6251. PMID: 20332208, PMCID: PMC2851968, DOI: 10.1073/pnas.0913531107.Peer-Reviewed Original ResearchConceptsPolyketide synthasesCrystal structureC bond formationPolyketide natural productsProduct release mechanismRing closure reactionAlpha/beta hydrolase foldSynthetic versatilitySynthetic potentialSubstrate-binding chamberIterative polyketide synthasesC cyclizationFatty acid synthasesBond formationClaisen cyclizationFirst mechanistic insightsProtein conformational changesNatural productsClosure reactionSubstrate positioningSide chainsBiosynthesis of aflatoxinSubstrate side chainDiverse architecturesPolyketide synthase A
This site is protected by hCaptcha and its Privacy Policy and Terms of Service apply