Addressing Serine Lability in a Paramagnetic Dimethyl
Sulfoxide Reductase Catalytic Intermediate
Posted on 10.06.2021 - 23:13
Two new desoxo molybdenum(V) complexes have been synthesized and characterized as models for the paramagnetic high-g split intermediate observed in the catalytic cycle of dimethyl sulfoxide reductase (DMSOR). Extended X-ray absorption fine structure (EXAFS) and electron paramagnetic resonance (EPR) data are used to provide new insight into the geometric and electronic structures of high-g split and other EPR-active type II/III DMSOR family enzyme forms. The results support a 6-coordinate [(PDT)2Mo(OH)(OSer)]− structure (PDT = pyranopterin dithiolene) for a high-g split with four S donors from two PDT ligands, a coordinated hydroxyl ligand, and a serinate O donor. This geometry orients the redox orbital toward the substrate access channel for the two-electron reduction of substrates.
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KC, Khadanand; Yang, Jing; Kirk, Martin L. (2021): Addressing Serine Lability in a Paramagnetic Dimethyl Sulfoxide Reductase Catalytic Intermediate. ACS Publications. Collection. https://doi.org/10.1021/acs.inorgchem.1c00940
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Martin L. Kirk