2014 REU Poster: Expression and Characterization of WT BMUL4434 from Burkholderia multivorans
Johnson, Santina C.
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Bacterial cytochrome c peroxidases (bCcPs) are di-heme enzymes that protect the cell from peroxide by reducing it to water. Alternatively, MauG is a di-heme enzyme that is similar in structure to bCcPs, yet is a poor peroxidase. Instead, MauG catalyzes the formation of tryptophan tryptophyl quinone (TTQ) the catalytic cofactor required for MADH. Previous work in the Elliott lab used bioinformatics to investigate how sequence divergence within peroxidase superfamily reflects functionality. The bioinformatics analysis led to the discovery of unreported di-heme enzymes found in all strains of Burkholderia. BMUL4434 from Burkholderia multivorans was gene synthesized and codon optimized for expression in E. coli. We expressed and purified WT BMUL4434 and obtained initial optical characterization to understand where it falls in the peroxidase superfamily.
Poster presentation at REU Summer's End Research Symposium, 2014, by REU participant Santina Johnson, Spring Hill College - Sean Elliott group, Kimberly Rizzolo lab mentor
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