Structure of 3-mercaptopropionic acid dioxygenase with a substrate analog reveals bidentate substrate binding at the iron center
Nicholas J. York, Molly M. Lockart, Sinjinee Sardar, Nimesh Khadka, Wuxian Shi, Ronald E. Stenkamp, Jianye Zhang, Philip D. Kiser, Brad S. Pierce
Abstract
-binding site. Supporting HYSCORE spectroscopic experiments were performed on the (3MPA/NO)-bound Av3MDO iron nitrosyl (S = 3/2) site. In combination with spectroscopic simulations and optimized DFT models, this work provides an experimentally verified model of the Av3MDO enzyme-substrate complex, effectively resolving a debate in the literature regarding the preferred substrate-binding denticity. These results elegantly explain the observed 3MDO substrate specificity, but leave unanswered questions regarding the mechanism of substrate-gated reactivity with dioxygen.
Topics & Concepts
ChemistryDenticitySubstrate (aquarium)Active siteCarboxylateStereochemistryLigand (biochemistry)DioxygenaseBinding siteCrystallographyCatalysisEnzymeCrystal structureOrganic chemistryBiochemistryReceptorGeologyOceanographyMetal-Catalyzed Oxygenation MechanismsMicrobial metabolism and enzyme functionVanadium and Halogenation Chemistry