File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Using xenon as a probe for dioxygen-binding sites in copper amine oxidases

TitleUsing xenon as a probe for dioxygen-binding sites in copper amine oxidases
Authors
Keywordscopper enzyme
xenon chamber
dioxygen binding
xenon-protein complex
amine oxidase
Issue Date2004
Citation
Journal of Molecular Biology, 2004, v. 344, n. 3, p. 599-607 How to Cite?
AbstractPotential 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 Identifierhttp://hdl.handle.net/10722/219824
ISSN
2015 Impact Factor: 4.517
2015 SCImago Journal Rankings: 3.002

 

DC FieldValueLanguage
dc.contributor.authorDuff, Anthony P.-
dc.contributor.authorTrambaiolo, Daniel M.-
dc.contributor.authorCohen, Aina E.-
dc.contributor.authorEllis, Paul J.-
dc.contributor.authorJuda, Gregory A.-
dc.contributor.authorShepard, Eric M.-
dc.contributor.authorLangley, David B.-
dc.contributor.authorDooley, David M.-
dc.contributor.authorFreeman, Hans C.-
dc.contributor.authorGuss, J. Mitchell-
dc.date.accessioned2015-09-23T02:58:02Z-
dc.date.available2015-09-23T02:58:02Z-
dc.date.issued2004-
dc.identifier.citationJournal of Molecular Biology, 2004, v. 344, n. 3, p. 599-607-
dc.identifier.issn0022-2836-
dc.identifier.urihttp://hdl.handle.net/10722/219824-
dc.description.abstractPotential 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.languageeng-
dc.relation.ispartofJournal of Molecular Biology-
dc.subjectcopper enzyme-
dc.subjectxenon chamber-
dc.subjectdioxygen binding-
dc.subjectxenon-protein complex-
dc.subjectamine oxidase-
dc.titleUsing xenon as a probe for dioxygen-binding sites in copper amine oxidases-
dc.typeArticle-
dc.description.natureLink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.jmb.2004.09.075-
dc.identifier.pmid15533431-
dc.identifier.scopuseid_2-s2.0-7944226404-
dc.identifier.volume344-
dc.identifier.issue3-
dc.identifier.spage599-
dc.identifier.epage607-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats