Dataset Information

Two-Step Azidoalkenylation of Terminal Alkenes Using Iodomethyl Sulfones.

ABSTRACT: The radical azidoalkylation of alkenes that was initially developed with ?-iodoesters and ?-iodoketones was extended to other activated iodomethyl derivatives. By using iodomethyl aryl sulfones, the preparation of ?-azidosulfones was easily achieved. Facile conversion of these azidosulfones to homoallylic azides using a Julia-Kocienski olefination reaction is reported, making the whole process equivalent to the azidoalkenylation of terminal alkenes.

SUBMITTER: Millius N

PROVIDER: S-EPMC6891591 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

Two-Step Azidoalkenylation of Terminal Alkenes Using Iodomethyl Sulfones.

Millius Nicolas N Lapointe Guillaume G Renaud Philippe P

Molecules (Basel, Switzerland) 20191118 22

The radical azidoalkylation of alkenes that was initially developed with α-iodoesters and α-iodoketones was extended to other activated iodomethyl derivatives. By using iodomethyl aryl sulfones, the preparation of γ-azidosulfones was easily achieved. Facile conversion of these azidosulfones to homoallylic azides using a Julia-Kocienski olefination reaction is reported, making the whole process equivalent to the azidoalkenylation of terminal alkenes. ...[more]

PMID: 31752245

Similar Datasets

Project description:BACKGROUND:P450 fatty acid decarboxylases represented by the unusual CYP152 peroxygenase family member OleTJE have been receiving great attention recently since these P450 enzymes are able to catalyze the simple and direct production of 1-alkenes for potential applications in biofuels and biomaterials. To gain more mechanistic insights, broader substrate spectra, and improved decarboxylative activities, it is demanded to discover and investigate more P450 fatty acid decarboxylases. RESULTS:Here, we describe for the first time the expression, purification, and in vitro biochemical characterization of two new CYP152 peroxygenases, CYP-Aa162 and CYP-Sm46?29, that are capable of decarboxylating straight-chain saturated fatty acids. Both enzymes were found to catalyze the decarboxylation and hydroxylation of a broad range of free fatty acids (C10-C20) with overlapping substrate specificity, yet distinct chemoselectivity. CYP-Sm46?29 works primarily as a fatty (lauric) acid decarboxylase (66.1 ± 3.9% 1-undecene production) while CYP-Aa162 more as a fatty (lauric) acid hydroxylase (72.2 ± 0.9% hydroxy lauric acid production). Notably, the optical spectroscopic analysis of functional CYP-Sm46?29 revealed no characteristic P450 band, suggesting a unique heme coordination environment. Active-site mutagenesis analysis showed that substitution with the proposed key decarboxylation-modulating residues, His85 and Ile170, enhanced the decarboxylation activity of CYP-Aa162 and P450BS?, emphasizing the importance of these residues in directing the decarboxylation pathway. Furthermore, the steady-state kinetic analysis of CYP-Aa162 and CYP-Sm46?29 revealed both cooperative and substrate inhibition behaviors which are substrate carbon chain length dependent. CONCLUSIONS:Our data identify CYP-Sm46?29 as an efficient OleTJE-like fatty acid decarboxylase. Oxidative decarboxylation chemoselectivity of the CYP152 decarboxylases is largely dependent upon the carbon chain length of fatty acid substrates and their precise positioning in the enzyme active site. Finally, the kinetic mode analysis of the enzymes could provide important guidance for future process design.

Dataset Information

Two-Step Azidoalkenylation of Terminal Alkenes Using Iodomethyl Sulfones.

Publications

Two-Step Azidoalkenylation of Terminal Alkenes Using Iodomethyl Sulfones.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets