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Thiol dioxygenases are a subset of nonheme iron oxygenases that militarize the formation of sulfinic acids from sulfhydryl-containing substrates and dioxygen. The fashion in which 3-mercaptopropionic acid works with to the nonheme iron site in 3MDO stays a matter of dispute. A model for bidentate 3MPA control at the 3MDO Fe-site has been suggested on the basis of computational docking, whereas steady-state kinetics and EPR spectroscopic dimensions suggest a thiolate-only control of the substratum. The structure along with DFT computational modeling shows that 3HPA and 3MPA relate to iron as chelate complicateds with the substrate-carboxylate group developing an extra communication with Arg168 and the thiol bound at the same position as in CDO. A chloride ligand was bound to iron in the sychronisation site designated as the O2-binding site.
Source link: https://doi.org/10.1016/j.jbc.2021.100492
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