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EXPLORING NOVEL REACTIVITY FOR ENGINEERED MYOGLOBINBIOCATALYST: [2,3] SIGMATROPIC REARRANGEMENT OF ALLYLIC ALCOHOLS

Abstract

Biocatalysis is a green, sustainable process in which enzymes, whole-cells or other biological catalysts perform a required synthetic transformation in a highly efficient manner. Recently, the heme protein myoglobin (Mb) has been emerged as a robust biocatalyst. The engineered versions of Mb biocatalyst have shown to perform non-native chemical transformations such as cyclopropanation of activated and unactivated alkenes, hetero-atom insertion (S-H, N-H) reactions etc. in very high yields and in excellent selectivity. Here, we explore the reactivity of engineered Mb variants toward the [2,3] sigmatropic rearrangement of allylic acetals and thioketals to provide a simple, environmentally friendly and sustainable route to synthetically useful multifunctional organic compounds. With the above goal in mind, a feasibility study was performed using acrolein dimethyl acetal and ethyl diazoacetate (EDA) in presence of engineered Mb catalyst, Mb H64V V68A. Along with preforming these reactions under anaerobic, semi-aerobic, and aerobic conditions, this study incorporates additionally diverse experimental and controlled variables such as concentrations of the substrate and enzyme, temperature, pH, time trials, and substrate ratios. Our hope is to explore the prime conditions for this engineered myoglobin biocatalyst and determine conditions that this enzyme is able to function optimally in. Gas chromatography (GC) and Gas chromatography-Mass spectrometry (GC-MS) were used to quantify the biocatalysis reaction yields, percent conversions, and reaction rates. Nuclear magnetic resonance spectroscopy (NMR) was used to characterize the standard products and the products obtained from enzyme reactions.

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