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- Publisher Website: 10.1016/j.jmb.2004.09.075
- Scopus: eid_2-s2.0-7944226404
- PMID: 15533431
- WOS: WOS:000225304500001
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Article: Using xenon as a probe for dioxygen-binding sites in copper amine oxidases
Title | Using xenon as a probe for dioxygen-binding sites in copper amine oxidases |
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Authors | |
Keywords | copper enzyme xenon chamber dioxygen binding xenon-protein complex amine oxidase |
Issue Date | 2004 |
Citation | Journal of Molecular Biology, 2004, v. 344, n. 3, p. 599-607 How to Cite? |
Abstract | Potential dioxygen-binding sites in three Cu amine oxidases have been investigated by recording X-ray diffraction data at 1.7-2.2 Å resolution for crystals under a high pressure of xenon gas. Electron-density difference maps and crystallographic refinement provide unequivocal evidence for a number of Xe-binding sites in each enzyme. Only one of these sites is present in all three Cu amine oxidases studied. Structural changes elsewhere in the protein molecules are insignificant. The results illustrate the use of xenon as a probe for cavities, in which a protein may accommodate a dioxygen molecule. The finding of a potential dioxygen-binding cavity close to the active site of Cu amine oxidases may be relevant to the function of the enzymes, since the formation of a transient protein-dioxygen complex is a likely step in the catalytic mechanism. No evidence was found for xenon binding in a region of the molecule that was previously identified in two other Cu amine oxidases as a potential transient dioxygen-binding site. © 2004 Elsevier Ltd. All rights reserved. |
Persistent Identifier | http://hdl.handle.net/10722/219824 |
ISSN | 2023 Impact Factor: 4.7 2023 SCImago Journal Rankings: 2.212 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Duff, Anthony P. | - |
dc.contributor.author | Trambaiolo, Daniel M. | - |
dc.contributor.author | Cohen, Aina E. | - |
dc.contributor.author | Ellis, Paul J. | - |
dc.contributor.author | Juda, Gregory A. | - |
dc.contributor.author | Shepard, Eric M. | - |
dc.contributor.author | Langley, David B. | - |
dc.contributor.author | Dooley, David M. | - |
dc.contributor.author | Freeman, Hans C. | - |
dc.contributor.author | Guss, J. Mitchell | - |
dc.date.accessioned | 2015-09-23T02:58:02Z | - |
dc.date.available | 2015-09-23T02:58:02Z | - |
dc.date.issued | 2004 | - |
dc.identifier.citation | Journal of Molecular Biology, 2004, v. 344, n. 3, p. 599-607 | - |
dc.identifier.issn | 0022-2836 | - |
dc.identifier.uri | http://hdl.handle.net/10722/219824 | - |
dc.description.abstract | Potential dioxygen-binding sites in three Cu amine oxidases have been investigated by recording X-ray diffraction data at 1.7-2.2 Å resolution for crystals under a high pressure of xenon gas. Electron-density difference maps and crystallographic refinement provide unequivocal evidence for a number of Xe-binding sites in each enzyme. Only one of these sites is present in all three Cu amine oxidases studied. Structural changes elsewhere in the protein molecules are insignificant. The results illustrate the use of xenon as a probe for cavities, in which a protein may accommodate a dioxygen molecule. The finding of a potential dioxygen-binding cavity close to the active site of Cu amine oxidases may be relevant to the function of the enzymes, since the formation of a transient protein-dioxygen complex is a likely step in the catalytic mechanism. No evidence was found for xenon binding in a region of the molecule that was previously identified in two other Cu amine oxidases as a potential transient dioxygen-binding site. © 2004 Elsevier Ltd. All rights reserved. | - |
dc.language | eng | - |
dc.relation.ispartof | Journal of Molecular Biology | - |
dc.subject | copper enzyme | - |
dc.subject | xenon chamber | - |
dc.subject | dioxygen binding | - |
dc.subject | xenon-protein complex | - |
dc.subject | amine oxidase | - |
dc.title | Using xenon as a probe for dioxygen-binding sites in copper amine oxidases | - |
dc.type | Article | - |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1016/j.jmb.2004.09.075 | - |
dc.identifier.pmid | 15533431 | - |
dc.identifier.scopus | eid_2-s2.0-7944226404 | - |
dc.identifier.volume | 344 | - |
dc.identifier.issue | 3 | - |
dc.identifier.spage | 599 | - |
dc.identifier.epage | 607 | - |
dc.identifier.isi | WOS:000225304500001 | - |
dc.identifier.issnl | 0022-2836 | - |