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Macrophomate synthase was touted by some as the first wellcharacterized Diels-Alderase enzyme, but evidence has been accumulated that indicates that the cyclization catalyzed by this enzyme is stepwise, and therefore not truly pericyclic. See, for example
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Macrophomate synthase was touted by some as the first wellcharacterized Diels-Alderase enzyme, but evidence has been accumulated that indicates that the cyclization catalyzed by this enzyme is stepwise, and therefore not truly pericyclic. See, for example: (a) Guimarães, C. R. W.; Udier-Blagovió, M.; Jorgensen, W. L. J. Am. Chem. Soc. 2005, 127, 3577-3588.
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All stationary points were characterized as minima or transition state structures by analyzing their vibrational frequencies. Intrinsic reaction coordinate (IRC) calculations
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All stationary points were characterized as minima or transition state structures by analyzing their vibrational frequencies. Intrinsic reaction coordinate (IRC) calculations (Gonzalez, C.; Schlegel, H. B. J. Phys. Chem. 1990, 94, 5523-5527.
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6 and MP2/6-31G(d) (Møller, C.; Plesset, M. S. Phys. Rev. 1934, 46, 618-622) were performed on some optimized B3LYP/6-31.G(d) geometries, as described in the text.
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note
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estert⋯ H distance was 0.1.2 Å longer in solvent than in the gas phase; changes to the bonds that form and break during the Diels-Alder reaction, as well as changes to the O-H bonds in the water molecule, were all well less than 0.01 A. The barrier computed with structures optimized in solvent was 27.0 kcal/mol, ∼0.4 kcal/mol lower than that computed with single-point energies (see Figure 2). For system K, full optimization of the transition state structure in solvent failed, since, after an initial period of structural optimization, the calculation consistently oscillated between structures extremely close in geometry and differing in energy by less than 0.02 kcal/mol. Using the structure with lower energy of these two and the fully optimized reactant, an upper limit for the barrier of 25.8 kcal/mol (not zero-point energy corrected) was computed; this value is only ∼0.2 kcal/mol lower than that calculated with single-point energies (see Figure 2). Here, the largest geometric differences between the transition state structures optimized in the gas phase and in solvent were found in the O ⋯ H-N substructure: the O⋯ H distance was 0.16 Ä longer and the H-N distance was 0.06 Å shorter in solvent than in the gas phase; changes to the bonds that form and break during the Diels-Alder reaction were all less than 0.025 Å. Thus, using solvent single-point energies to compute barriers seems reasonable. The structural drawing in Figure 3 was produced using Ball & Stick (Müller, N.; Falk, A. Ball & Stick V.3.7.6, molecular graphics application for MacOS computers; Johannes Kepler University: Linz, Austria, 2000).
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The furan ring was replaced by a hydrogen atom in order to reduce the time required for computations (this ring system would add five nonhydrogen atoms and some conformational flexibility). We feel that this approach is reasonable since the furan ring is not directly conjugated to any of the π-systems present in the salvileucalins
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The furan ring was replaced by a hydrogen atom in order to reduce the time required for computations (this ring system would add five nonhydrogen atoms and some conformational flexibility). We feel that this approach is reasonable since the furan ring is not directly conjugated to any of the π-systems present in the salvileucalins.
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Note that all of the reactions in Figure 1 are predicted to be exothermic; trading π-bonds for σ-bonds counteracts the increase in strain upon cycloaddition
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Note that all of the reactions in Figure 1 are predicted to be exothermic; trading π-bonds for σ-bonds counteracts the increase in strain upon cycloaddition.
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11 all energies (B3LYP/ 6-31G(d)+0.9806ZPE) are in kcal/mol): "Figure Presented"
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11 all energies (B3LYP/ 6-31G(d)+0.9806ZPE) are in kcal/mol): "Figure Presented"
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