DC Field | Value | Language |
---|---|---|
dc.contributor.author | Gherman, BF | ko |
dc.contributor.author | Baik, Mu-Hyun | ko |
dc.contributor.author | Lippard, SJ | ko |
dc.contributor.author | Friesner, RA | ko |
dc.date.accessioned | 2016-04-12T07:46:27Z | - |
dc.date.available | 2016-04-12T07:46:27Z | - |
dc.date.created | 2015-09-11 | - |
dc.date.created | 2015-09-11 | - |
dc.date.issued | 2004-03 | - |
dc.identifier.citation | JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, v.126, no.9, pp.2978 - 2990 | - |
dc.identifier.issn | 0002-7863 | - |
dc.identifier.uri | http://hdl.handle.net/10203/203360 | - |
dc.description.abstract | 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 a ferromagnetically coupled diiron(II,III) H-superoxo structure, which undergoes intersystem crossing to the antiferromagnetic surface and affords H-peroxo, a symmetric diiron(III) unit with a nonplanar mu-eta(2):eta(2)-O2- binding mode. Homolytic cleavage of the O-O bond yields the catalytically competent intermediate 0, which has a di (mu-oxo)diiron(IV) core. A carboxylate shift involving Glu243 is essential to the formation of the symmetric Hperoxo and Q structures. Both thermodynamic and kinetic features agree well with experimental data, and computed spin-exchange coupling constants are in accord with spectroscopic values. Evidence is presented for pH-independent decay of H-red and H-peroxo. Key electron-transfer steps that occur in the course of generating Q from H-red are also detailed and interpreted. In contrast to prior theoretical studies, a requisite large model has been employed, electron spins and couplings have been treated in a quantitative manner, potential energy surfaces have been extensively explored, and quantitative total energies have been determined along the reaction pathway. | - |
dc.language | English | - |
dc.publisher | AMER CHEMICAL SOC | - |
dc.subject | METHYLOCOCCUS-CAPSULATUS BATH | - |
dc.subject | METHYLOSINUS-TRICHOSPORIUM OB3B | - |
dc.subject | EFFECTIVE CORE POTENTIALS | - |
dc.subject | NONHEME DIIRON ENZYMES | - |
dc.subject | DINUCLEAR IRON CENTERS | - |
dc.subject | O BOND-CLEAVAGE | - |
dc.subject | C-H BOND | - |
dc.subject | HYDROXYLASE COMPONENT | - |
dc.subject | INTERMEDIATE-Q | - |
dc.subject | MOLECULAR CALCULATIONS | - |
dc.title | Dioxygen activation in methane monooxygenase: A theoretical study | - |
dc.type | Article | - |
dc.identifier.wosid | 000220038800062 | - |
dc.identifier.scopusid | 2-s2.0-1542377662 | - |
dc.type.rims | ART | - |
dc.citation.volume | 126 | - |
dc.citation.issue | 9 | - |
dc.citation.beginningpage | 2978 | - |
dc.citation.endingpage | 2990 | - |
dc.citation.publicationname | JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | - |
dc.identifier.doi | 10.1021/ja03506+ | - |
dc.contributor.localauthor | Baik, Mu-Hyun | - |
dc.contributor.nonIdAuthor | Gherman, BF | - |
dc.contributor.nonIdAuthor | Lippard, SJ | - |
dc.contributor.nonIdAuthor | Friesner, RA | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | METHYLOCOCCUS-CAPSULATUS BATH | - |
dc.subject.keywordPlus | METHYLOSINUS-TRICHOSPORIUM OB3B | - |
dc.subject.keywordPlus | EFFECTIVE CORE POTENTIALS | - |
dc.subject.keywordPlus | NONHEME DIIRON ENZYMES | - |
dc.subject.keywordPlus | DINUCLEAR IRON CENTERS | - |
dc.subject.keywordPlus | O BOND-CLEAVAGE | - |
dc.subject.keywordPlus | C-H BOND | - |
dc.subject.keywordPlus | HYDROXYLASE COMPONENT | - |
dc.subject.keywordPlus | INTERMEDIATE-Q | - |
dc.subject.keywordPlus | MOLECULAR CALCULATIONS | - |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.