We are proud to share our new publication titled “Improved resolution of 3-mercaptopropionate dioxygenase active site provided by ENDOR spectroscopy offers insight into catalytic mechanism” J Biol Chem. 2024: DOI: https://doi.org/10.1016/j.jbc.2024.105777. This report represents the culmination of our investigation into the catalytic role of conserved hydrogen bonding interactions within the thiol dioxygenase active site. Here, 1H Mims ENDOR spectroscopy was used to validate DFT computational models for the MDO active site simultaneously coordinated by substrate and nitric oxide. As the structure for this iron-nitrosyl is believed to mimic iron-oxo intermediates within the MDO catalytic cycle, this model provides a framework for discussion of the oxygenation mechanism.

On September 9, 2023 the Pierce group received an award (2R15GM117511-04) for $413,696 from National Institutes of Health-General Medical Sciences. This work supports the ongoing efforts of the Pierce group to investigate how weak outer-sphere interactions influence reactivity among the thiol dioxygenase class of enzymes.