Oxidative desulfurization (ODS) reactions are used to remove sulfur from hydrocarbon fuels, which is considered a more environmentally benign alternative to hydrodesulfurization reactions. One class of catalysts that carry out this reaction in the presence of an oxidant (e.g. H<sub>2</sub>O<sub>2</sub> or mCPBA) is hemoproteins such as myoglobin and hemoglobin. However, unlike their Fe porphyrin analogue, Mn porphyrins in general tend to be more efficient for catalyzing substrate oxidation and produce higher yields. In this work, we will utilize manganese myoglobin (MnMb), which naturally forms a Mn-N(Histidine) bond interaction that is crucial for generating a high valent Mn=O intermediate. Its optical properties in solution and in a silica sol-gel matrix (which increases stability without compromising its catalytic properties) are studied using UV-Vis and IR spectroscopies. ODS reactions are carried out with dibenzothiophene as a substrate, and the reaction mixture will be tested for sulfones using LC-MS and NMR spectroscopies. Future work will involve investigating the kinetics of the ODS reaction as catalyzed by the artificial Mb system.

Characterizing manganese myoglobin in solution and in sol-gel towards its use in oxidative desulfurization reactions

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