Daniel Murray (PhD candidate)
CMB graduate student in the Stroupe Lab.

Daniel Murray (PhD candidate) CMB graduate student in the Stroupe Lab. Daniel Murray is a CMB PhD candidate in the Stroupe Lab studying the structure and function of the bacterial sulfur metabolizing machinery sulfite reductase (SiR). SiR is a flexible metalloflavoprotein that catalyzes an efficient six-electron reduction of sulfur to prepare it for assimilation into biomass such as cysteine and methionine. Efforts to understand SiR and other metabolic oxidoreductases have the potential to inform synthetic enzyme design for environmental bioremediation of oxyanion pollutants as well as our basic understanding of enzyme function. Daniel uses neutron scattering of SiR proteins in solution through a collaboration with Oak Ridge National Laboratory to circumvent SiR’s recalcitrance to most other structural biology techniques. Daniel’s doctoral research provided solution structures of SiR monomers and heterodimers, which enabled insights into the effects of complex assembly and changes in redox state on SiR. Additionally, his neutron scattering work provided a solution-state characterization of dodecameric SiR holoenzyme that may contribute to our understanding of the complex’s efficiency. Recent publication: Murray, D., Weiss, K., Stanley, C., Nagy, G. & Stroupe, M. E. Small-angle neutron scattering solution structures of NADPH-dependent sulfite reductase. Journal of Structural Biology 213, 107724, doi:https://doi.org/10.1016/j.jsb.2021.107724 (2021).