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http://hdl.handle.net/2445/127866
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DC Field | Value | Language |
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dc.contributor.author | Cowley, Ryan E. | - |
dc.contributor.author | Cirera Fernández, Jordi | - |
dc.contributor.author | Qayyum, Munzarin F. | - |
dc.contributor.author | Rokhsana, Dalia | - |
dc.contributor.author | Hedman, Britt | - |
dc.contributor.author | Hodgson, Keith O. | - |
dc.contributor.author | Dooley, David M. | - |
dc.contributor.author | Solomon, Edward I. | - |
dc.date.accessioned | 2019-02-04T15:36:36Z | - |
dc.date.available | 2019-02-04T15:36:36Z | - |
dc.date.issued | 2016-09-14 | - |
dc.identifier.issn | 0002-7863 | - |
dc.identifier.uri | http://hdl.handle.net/2445/127866 | - |
dc.description.abstract | Galactose oxidase (GO) is a copper-dependent enzyme that accomplishes 2e- substrate oxidation by pairing a single copper with an unusual cysteinylated tyrosine (Cys-Tyr) redox cofactor. Previous studies have demonstrated that the post-translational biogenesis of Cys-Tyr is copper- and O2-dependent, resulting in a self-processing enzyme system. To investigate the mechanism of cofactor biogenesis in GO, the active-site structure of Cu(I)-loaded GO was determined using X-ray absorption near edge structure (XANES) and extended X-ray absorption fine structure (EXAFS) spectroscopy, and density-functional theory (DFT) calculations were performed on this model. Our results show that the active-site tyrosine lowers the Cu potential to enable the thermodynamically unfavorable 1e- reduction of O2, and the resulting Cu(II)-O2¿- is activated toward H atom abstraction from cysteine. The final step of biogenesis is a concerted reaction involving coordinated Tyr ring deprotonation where Cu(II) coordination enables formation of the Cys-Tyr cross-link. These spectroscopic and computational results highlight the role of the Cu(I) in enabling O2 activation by 1e- and the role of the resulting Cu(II) in enabling substrate activation for biogenesis. | - |
dc.format.extent | 11 p. | - |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | - |
dc.publisher | American Chemical Society | - |
dc.relation.isformatof | Versió postprint del document publicat a: https://doi.org/10.1021/jacs.6b05792 | - |
dc.relation.ispartof | Journal of the American Chemical Society, 2016, vol. 138, num. 40, p. 13219-13229 | - |
dc.relation.uri | https://doi.org/10.1021/jacs.6b05792 | - |
dc.rights | (c) American Chemical Society , 2016 | - |
dc.source | Articles publicats en revistes (Química Inorgànica i Orgànica) | - |
dc.subject.classification | Enzims | - |
dc.subject.classification | Transport d'electrons | - |
dc.subject.classification | Catàlisi | - |
dc.subject.other | Enzymes | - |
dc.subject.other | Electron transport | - |
dc.subject.other | Catalysis | - |
dc.title | Structure of the Reduced Copper Active Site in Pre-Processed Galactose Oxidase: Ligand Tuning for One-Electron O2 Activation in Cofactor Biogenesis | - |
dc.type | info:eu-repo/semantics/article | - |
dc.type | info:eu-repo/semantics/acceptedVersion | - |
dc.identifier.idgrec | 667316 | - |
dc.date.updated | 2019-02-04T15:36:36Z | - |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | - |
dc.identifier.pmid | 27626829 | - |
Appears in Collections: | Articles publicats en revistes (Química Inorgànica i Orgànica) |
Files in This Item:
File | Description | Size | Format | |
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667316.pdf | 1.69 MB | Adobe PDF | View/Open |
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