title: Synthesis, characterization, electrochemistry, electronic structure, and isomerization of mononuclear oxo-molybdenum(V) complexes: the serine gate hypothesis in the function of DMSO reductases.
abstract: Crystal structures of DMSO reductases isolated from two different sources and the crystal structure of related trimethylamine-N-oxide reductase indicate that the angle between the terminal oxo atom on the molybdenum and the serinato oxygen varies significantly. To understand the significance of this angular variation, we have synthesized two isomeric compounds of the heteroscorpionato ligand (L1OH) (cis- and trans-(L1O)Mo(V)OCl(2)), where the phenolic oxygen mimics the serinato oxygen donor. Density functional and semiempirical calculations indicate that the trans isomer is more stable than the cis. The lower stability of the cis isomer can be attributed to two factors. First, a strong antibonding interaction between the phenolic oxygen with molybdenum d(xy) orbital raises the energy of this orbital. Second, the strong trans influence of the terminal oxo group in the trans isomer places the phenol ring, and hence the bulky tertiary butyl group, in a less sterically hindered position. In solution, the cis isomer spontaneously converts to the thermodynamically favorable trans isomer. This geometric transformation follows a first-order process, with an enthalpy of activation of 20 kcal/mol and an entropy of activation of -9 cal/mol K. Computational analysis at the semiempirical level supports a twist mechanism as the most favorable pathway for the geometric transformation. The twist mechanism is further supported by detailed mass spectral data collected in the presence of excess tetraalkylammonium salts. Both the cis and trans isomers exhibit well-defined one-electron couples due to the reduction of molybdenum(V) to molybdenum(IV), with the cis isomer being more difficult to reduce. Both isomers also exhibit oxidative couples because of the oxidation of molybdenum(V) to molybdenum(VI), with the cis isomer being easier to oxidize. This electrochemical behavior is consistent with a higher-energy redox orbital in the cis isomer, which has been observed computationally. Collectively, this investigation demonstrates that by changing the O(t)-Mo-O(p) angle, the reduction potential can be modulated. This geometrically controlled modulation may play a gating role in the electron-transfer process during the regeneration steps in the catalytic cycle.
authors.affiliation: Department of Chemistry and Biochemistry, Duquesne University, Pittsburgh, Pennsylvania 15282, USA.
authors.forename: Brian
authors.initials: B
authors.lastname: Kail
authors.forename: Victor N
authors.initials: VN
authors.lastname: Nemykin
authors.forename: Scott R
authors.initials: SR
authors.lastname: Davie
authors.forename: Carl J
authors.initials: CJ
authors.lastname: Carrano
authors.forename: Brian
authors.initials: B
authors.lastname: Hammes
authors.forename: Partha
authors.initials: P
authors.lastname: Basu
mesh_terms: D001665:Binding Sites; D002384:Catalysis; D018360:Crystallography, X-Ray; D004563:Electrochemistry; D007506:Iron-Sulfur Proteins; D007700:Kinetics; D008956:Models, Chemical; D015394:Molecular Structure; D009247:NADH, NADPH Oxidoreductases / Q000737:chemistry; D009942:Organometallic Compounds / Q000138:chemical synthesis*; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000737:chemistry*; D000587:Oxidoreductases Acting on CH-NH Group Donors; D012694:Serine; D021241:Spectrometry, Mass, Electrospray Ionization; D017550:Spectroscopy, Fourier Transform Infrared; D013237:Stereoisomerism
chemical_list: D007506:Iron-Sulfur Proteins; D009942:Organometallic Compounds; D012694:Serine; D010088:Oxidoreductases; C021567:methylamine dehydrogenase; D000587:Oxidoreductases Acting on CH-NH Group Donors; D009247:NADH, NADPH Oxidoreductases; C045664:dimethyl sulfoxide reductase