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Short article pubs.acs.org/JACSOpen Access on 06/02/Sulfur KEdge Xray Absorption Spectroscopy and Density Functional Theory Calculations on Monooxo MoIV and Bisoxo MoVI Bisdithiolenes: Insights in to the Mechanism of Oxo Transfer in Sulfite Oxidase and Its Relation for the Mechanism of DMSO ReductaseYang Ha, Adam L. Tenderholt,, Richard H. Holm,*,?Britt Hedman,*, Keith O. Hodgson,*,, and Edward I. Solomon*,,Division of Chemistry, Stanford University, Stanford, California 94305, United states Stanford Synchrotron Radiation Lightsource, SLAC, Stanford University, Menlo Park, California 94025, Usa ?Division of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, United StatesS * Supporting InformationABSTRACT: Sulfur K-edge X-ray absorption spectroscopy (XAS) and density functional theory (DFT) calculations have already been used to ascertain the electronic structures of two complexes [MoIVO(bdt)2]2- and [MoVIO2(bdt)2]2- (bdt = benzene-1,2-dithiolate(2-)) that relate towards the lowered and oxidized types of sulfite oxidase (SO). These are compared with those of previously studied dimethyl sulfoxide reductase (DMSOr) models. DFT calculations supported by the data are extended to evaluate the reaction coordinate for oxo transfer to a phosphite ester substrate. Three doable transition states are identified using the a single at lowest energy, stabilized by a P-S interaction, in very good agreement with experimental kinetics information. Comparison of each oxo transfer reactions shows that in DMSOr, exactly where the oxo is transferred in the substrate to the metal ion, the oxo transfer induces electron transfer, although in SO, where the oxo transfer is in the metal web page towards the substrate, the electron transfer initiates oxo transfer. This difference in reactivity is connected towards the difference in frontier molecular orbitals (FMO) on the metal-oxo and substrate-oxo bonds. Ultimately, these experimentally connected calculations are extended to oxo transfer by sulfite oxidase.Formula of 2-(4-Hydroxy-1H-indol-3-yl)acetic acid The presence of only one particular dithiolene at the enzyme active website selectively activates the equatorial oxo for transfer, and permits facile structural reorganization during turnover.83947-59-5 Chemscene 1. INTRODUCTION Molybdenum will be the one second row transition metal that has been found in practically all types of life, such as microorganisms, plants and animals.1 It can be a part of a multinuclear active website within the FeMoco cofactor in nitrogenase,two,three even though most other enzymes possess a mononuclear center, that is redoxactive between the MoIV and MoVI oxidation states and has pyranopterin-dithiolene ligands.PMID:24834360 4-7 The MoV oxidation state just isn’t straight involved inside the oxo transfer reaction, but is involved as enzymes and models cycle involving MoIV (d2) and MoVI (d0) oxidation states.eight These mononuclear molybdenum enzymes happen to be divided into three families: dimethyl sulfoxide (DMSO) reductases, sulfite oxidases, and xanthine oxidases.6 DMSO reductase and sulfite oxidase catalyze oxotransfer reactions. DMSO reductase reduces DMSO to DMS (dimethyl sulfide), with oxo transfer for the Mo center, which converts from a MoIV desoxo (i.e., no oxo ligand, but a with an alkoxide-Mo bond) to a MoVI monooxo species. Sulfite oxidase (SO) transfers an oxo ligand to substrates, converting the Mo center from a MoVI bisoxo to a MoIV monooxo species.?2014 American Chemical SocietyModel complexes have been synthesized and characterized that mimic either the structure and/or activity for these enzyme active sit.
