Living organisms are able to harness the power of light by using proteins known as photoreceptors which sense light with a molecule called a chromophore. For her postdoc research at The Hebrew University of Jerusalem’s Fritz Haber Center for Molecular Dynamics, Institute of Chemistry, Dr. Megan J. (Toda) Mackintosh studies one representative protein, the cyanobacteriochrome (CBCR) photoreceptor. Subfamilies with far-red–sensing (frCBCRs) capabilities were recently discovered, extending the range of the spectrum that can be sensed. This capability is highly sought after in optogenetics and other biomedical applications, because light of this wavelength can easily penetrate through skin. Dr. Mackintosh investigates this unusual far-red shifted spectrum, studying its protein-chromophore interactions in the hope of designing mutants with enhanced photochemical properties.
Dr. Mackintosh’s PhD in Theoretical Chemistry is from the University of Louisville. She performed electronic structure calculations on biologically important systems, including the B12 family of molecules known as cobalamins, which have light-sensitive properties that could be tapped for various applications in optogenetics, as well as for light-activated drug design.
Already as an undergraduate, Dr. Mackintosh designed a laboratory experiment to study hydrogen bonding in phenols, and published her work in the American Chemical Society’s Journal of Chemical Education.
As president of the Chemistry Graduate Student Association at the University of Louisville, Dr. Mackintosh says she learned that leading isn’t just about planning—it’s about empathy and keeping a group together, too.