Mechanistic Analysis of Nucleophilic Substrates Oxidation by Functional Models of Vanadium-Dependent Haloperoxidases: A Density Functional Theory Study
dc.contributor.author | Schneider, Curtis J. | en_US |
dc.contributor.author | Zampella, Giuseppe | en_US |
dc.contributor.author | Greco, Claudio | en_US |
dc.contributor.author | Pecoraro, Vincent L. | en_US |
dc.contributor.author | De Gioia, Luca | en_US |
dc.date.accessioned | 2007-09-20T18:19:24Z | |
dc.date.available | 2008-04-03T18:52:11Z | en_US |
dc.date.issued | 2007-02 | en_US |
dc.identifier.citation | Schneider, Curtis J.; Zampella, Giuseppe; Greco, Claudio; Pecoraro, Vincent L.; De Gioia, Luca (2007). "Mechanistic Analysis of Nucleophilic Substrates Oxidation by Functional Models of Vanadium-Dependent Haloperoxidases: A Density Functional Theory Study." European Journal of Inorganic Chemistry 2007(4): 515-523. <http://hdl.handle.net/2027.42/55972> | en_US |
dc.identifier.issn | 1434-1948 | en_US |
dc.identifier.issn | 1099-0682 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/55972 | |
dc.description.abstract | Density functional theory has been used to investigate the structural, electronic, and reactivity properties of an established functional model for vanadium-dependent haloperoxidases, K[VO(O 2 )Hheida] (Hheida 2– = 2,2′-[(2-hydroxyethyl)imino]diacetate). Possible solution species were determined on the basis of potential exogenous donors present under the conditions necessary for reactivity. The energetically favored solution-state species is a 1:1 complex of Hheida and vanadium with a coordinated hydroxyethyl donor trans to the vanadium–oxido bond which is in agreement with the reported solid-state structure for K[VO(O 2 )Hheida]. Transition states of the oxidation reaction were located for four substrates: chloride, bromide, iodide, and dimethyl sulfide. The role of protonation and its effects on reactivity were examined for each substrate. Protonation of the peroxido moiety leads to a significant drop in the activation barrier for oxidation. In contrast no transition states could be located for an oxido-transfer process involving the oxido ligand. Barriers of activation calculated for halide oxidation were similar, providing support to the hypothesis that the p K a of the halide in acetonitrile is responsible for the decrease in reactivity between I – , Br – , and Cl – . The results presented herein provide a mechanistic correlation between a functional model and the enzyme, making K[VO(O 2 )Hheida] a “complete” functional model for vanadium-dependent haloperoxidase.(© Wiley-VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2007) | en_US |
dc.format.extent | 186221 bytes | |
dc.format.extent | 3118 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.publisher | WILEY-VCH Verlag | en_US |
dc.subject.other | Chemistry | en_US |
dc.subject.other | General Chemistry | en_US |
dc.title | Mechanistic Analysis of Nucleophilic Substrates Oxidation by Functional Models of Vanadium-Dependent Haloperoxidases: A Density Functional Theory Study | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Chemical Engineering | en_US |
dc.subject.hlbsecondlevel | Chemistry | en_US |
dc.subject.hlbsecondlevel | Materials Science and Engineering | en_US |
dc.subject.hlbtoplevel | Engineering | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Department of Chemistry, University of Michigan, Ann Arbor, Michigan, 48109-1055, USA | en_US |
dc.contributor.affiliationum | Department of Chemistry, University of Michigan, Ann Arbor, Michigan, 48109-1055, USA ; Biophysics Research Division, University of Michigan, Ann Arbor, Michigan, 48109-1055, USA ; | en_US |
dc.contributor.affiliationum | Department of Biotechnology and Biosciences, University of Milano-Bicocca, Piazza della Scienza 2, 20126 Milano, Italy ; | en_US |
dc.contributor.affiliationother | Department of Biotechnology and Biosciences, University of Milano-Bicocca, Piazza della Scienza 2, 20126 Milano, Italy | en_US |
dc.contributor.affiliationother | Department of Biotechnology and Biosciences, University of Milano-Bicocca, Piazza della Scienza 2, 20126 Milano, Italy | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/55972/1/515_ftp.pdf | en_US |
dc.identifier.doi | http://dx.doi.org/10.1002/ejic.200600739 | en_US |
dc.identifier.source | European Journal of Inorganic Chemistry | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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