Benjamin F. Gherman

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Using broken-symmetry unrestricted Density Functional Theory, the mechanism of enzymatic dioxygen activation by the hydroxylase component of soluble methane monooxygenase (MMOH) is determined to atomic detail. After a thorough examination of mechanistic alternatives, an optimal pathway was identified. The diiron(II) state H(red) reacts with dioxygen to give(More)
The electronic structures of key species involved in methane hydroxylation performed by the hydroxylase component of soluble methane monooxygenase (sMMO), as proposed previously on the basis of high-level density functional theory, were investigated. The reaction starts with initial approach of methane at one of the bridging oxo atoms in intermediate Q, a(More)
The origin of the substantial difference in deacylation rates for acyl-enzyme intermediates in penicillin-binding proteins (PBPs) and beta-lactamases has remained an unsolved puzzle whose solution is of great importance to understanding bacterial antibiotic resistance. In this work, accurate, large-scale mixed ab initio quantum mechanical/molecular(More)
Using broken-symmetry unrestricted density functional theory quantum mechanical (QM) methods in concert with mixed quantum mechanics/molecular mechanics (QM/MM) methods, the hydroxylation of methane and substituted methanes by intermediate Q in methane monooxygenase hydroxylase (MMOH) has been quantitatively modeled. This protocol allows the protein(More)
The character of singlet (C(3)N(2)H(5))CuO(2) ranges smoothly between copper(III) peroxide and copper(II) superoxide with variation of the electronic character of the supporting beta-diketiminate ligand. Over the range of the variation, multireference second-order perturbation theory predicts the (1)A(1) singlet state always to be lower in energy than the(More)
Copper(I) complexes of sterically hindered anilido imine ligands o-C6H4{N(C6H3(i)Pr2)}{C(R)=NC6H3(i)Pr2}- (L(1), R = H; L(2), R = CH3) have been prepared and characterized by spectroscopic and X-ray crystallographic methods. These complexes are highly reactive with O2, and in the case of L2 the product of low-temperature oxygenation was fully characterized(More)
The activation of dioxygen by dopamine beta-monooxygenase (DbetaM) and peptidylglycine alpha-hydroxylating monooxygenase (PHM) is postulated to occur at a copper site ligated by two histidine imidazoles and a methionine thioether, which is unusual because such thioether ligation is not present in other O2-activating copper proteins. To assess the possible(More)
The finding that dioxygen binds end-on to the Cu(B) site in the crystal structure of a precatalytic complex of peptidylglycine alpha-hydroxylating monooxygenase has spurred the search for biomimetic model complexes exhibiting the same dioxygen coordination. Recent work has not only indicated that sterically hindered beta-diketiminate ligands (L(1)) could(More)
To evaluate the fundamental process of O(2) activation at a single copper site that occurs in biological and catalytic systems, a detailed study of O(2) binding to Cu(I) complexes of beta-diketiminate ligands L (L(1) = backbone Me; L(2) = backbone tBu) by X-ray crystallography, X-ray absorption spectroscopy (XAS), cryogenic stopped-flow kinetics, and(More)
The tendency for mixed-isotope O2 fragments to exhibit different stretching frequencies in asymmetric environments is examined with various levels of electronic structure theory for simple peroxides and peroxyl radicals, as well as for a variety of monocopper-O2 complexes. The study of the monocopper species is motivated by their relevance to the active(More)