DC Field | Value | Language |
---|---|---|
dc.contributor.author | Lee, Yunho | ko |
dc.contributor.author | Lee, DH | ko |
dc.contributor.author | Sarjeant, AAN | ko |
dc.contributor.author | Zakharov, LN | ko |
dc.contributor.author | Rheingold, AL | ko |
dc.contributor.author | Karlin, KD | ko |
dc.date.accessioned | 2013-03-07T16:35:09Z | - |
dc.date.available | 2013-03-07T16:35:09Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2006-12 | - |
dc.identifier.citation | INORGANIC CHEMISTRY, v.45, no.25, pp.10098 - 10107 | - |
dc.identifier.issn | 0020-1669 | - |
dc.identifier.uri | http://hdl.handle.net/10203/90689 | - |
dc.description.abstract | To model thioether-copper coordination chemistry including oxidative reactivity, such as occurs in the copper monooxygenases peptidylglycine alpha-hydroxylating monooxygenase (PHM) and dopamine beta-hydroxylase (D beta H), we have synthesized new tridentate N2S ligands L-SEP and L-SBz [L-SEP = methyl(2-phenethylsulfanylpropyl)(2-pyridin-2-ylethyl) amine; LSBz) (2-benzylsulfanylpropyl)methyl(2-pyridin-2-ylethyl)amine)]. Both copper(I) and copper(II) complexes have been prepared, and their respective O-2 and H2O2 chemistry has been studied. Under mild conditions, oxygenation of [(L-SEP) Cu-I](+) (1a) and [(L-SBz)Cu-I](+) (2a) leads to ligand sulfoxidation, thus exhibiting copper monooxygenase activity. A copper(II) complex of this sulfoxide ligand product, [(L-SOEP)Cu-II(CH3OH)(OClO3)(2)], has been structurally characterized, demonstrating Cu-O-sulfoxide ligation. The X-ray structure of [(L-SEP)Cu-II(H2O)(OClO3)](+) (1b) and its solution UV-visible spectral properties [S-Cu-II LMCT band at 365 nm (MeCN solvent); epsilon = 4285 M-1 cm(-1)] indicate the thioether sulfur atom is bound to the cupric ion in both the solid (Cu-II-S distance: 2.31 angstrom) and solution states. Reaction of 1b with H2O2 leads to sulfonation via the sulfoxide; excess hydrogen peroxide gives mostly sulfone product. These results may provide some insight into recent reports concerning protein methionine oxidation, showing the potential importance of copper-mediated oxidation processes in certain biological settings. | - |
dc.language | English | - |
dc.publisher | AMER CHEMICAL SOC | - |
dc.subject | ALPHA-HYDROXYLATING MONOOXYGENASE | - |
dc.subject | DOPAMINE BETA-MONOOXYGENASE | - |
dc.subject | METHIONINE OXIDATION | - |
dc.subject | ELECTRON-TRANSFER | - |
dc.subject | CATALYTIC MECHANISM | - |
dc.subject | DIOXYGEN-BINDING | - |
dc.subject | PEPTIDYLGLYCINE MONOOXYGENASE | - |
dc.subject | AROMATIC HYDROXYLATION | - |
dc.subject | PHYSICAL PARAMETERS | - |
dc.subject | THIANTHRENE 5-OXIDE | - |
dc.title | Thioether sulfur oxygenation from O-2 or H2O2 reactivity of copper complexes with tridentate N2Sthioether ligands | - |
dc.type | Article | - |
dc.identifier.wosid | 000242479700027 | - |
dc.identifier.scopusid | 2-s2.0-33846136924 | - |
dc.type.rims | ART | - |
dc.citation.volume | 45 | - |
dc.citation.issue | 25 | - |
dc.citation.beginningpage | 10098 | - |
dc.citation.endingpage | 10107 | - |
dc.citation.publicationname | INORGANIC CHEMISTRY | - |
dc.identifier.doi | 10.1021/ic060730t | - |
dc.contributor.localauthor | Lee, Yunho | - |
dc.contributor.nonIdAuthor | Lee, DH | - |
dc.contributor.nonIdAuthor | Sarjeant, AAN | - |
dc.contributor.nonIdAuthor | Zakharov, LN | - |
dc.contributor.nonIdAuthor | Rheingold, AL | - |
dc.contributor.nonIdAuthor | Karlin, KD | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | ALPHA-HYDROXYLATING MONOOXYGENASE | - |
dc.subject.keywordPlus | DOPAMINE BETA-MONOOXYGENASE | - |
dc.subject.keywordPlus | METHIONINE OXIDATION | - |
dc.subject.keywordPlus | ELECTRON-TRANSFER | - |
dc.subject.keywordPlus | CATALYTIC MECHANISM | - |
dc.subject.keywordPlus | DIOXYGEN-BINDING | - |
dc.subject.keywordPlus | PEPTIDYLGLYCINE MONOOXYGENASE | - |
dc.subject.keywordPlus | AROMATIC HYDROXYLATION | - |
dc.subject.keywordPlus | PHYSICAL PARAMETERS | - |
dc.subject.keywordPlus | THIANTHRENE 5-OXIDE | - |
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