Show simple item record

dc.contributor.authorPenttinen, L
dc.contributor.authorRutanen, C
dc.contributor.authorSaloheimo, M
dc.contributor.authorKruus, K
dc.contributor.authorRouvinen, J
dc.contributor.authorHakulinen, N
dc.date.accessioned2018-05-14T09:06:50Z
dc.date.available2018-05-14T09:06:50Z
dc.date.issued2018
dc.identifier.urihttps://erepo.uef.fi/handle/123456789/6595
dc.description.abstractCoupled binuclear copper (CBC) enzymes have a conserved type 3 copper site that binds molecular oxygen to oxidize various mono- and diphenolic compounds. In this study, we found a new crystal form of catechol oxidase from Aspergillus oryzae (AoCO4) and solved two new structures from two different crystals at 1.8-Å and at 2.5-Å resolutions. These structures showed different copper site forms (met/deoxy and deoxy) and also differed from the copper site observed in the previously solved structure of AoCO4. We also analysed the electron density maps of all of the 56 CBC enzyme structures available in the protein data bank (PDB) and found that many of the published structures have vague copper sites. Some of the copper sites were then re-refined to find a better fit to the observed electron density. General problems in the refinement of metalloproteins and metal centres are discussed.
dc.language.isoEN
dc.publisherPublic Library of Science (PLoS)
dc.relation.ispartofseriesPLOS ONE
dc.relation.urihttp://dx.doi.org/10.1371/journal.pone.0196691
dc.rightsCC BY http://creativecommons.org/licenses/by/4.0/
dc.titleA new crystal form of Aspergillus oryzae catechol oxidase and evaluation of copper site structures in coupled binuclear copper enzymes
dc.description.versionpublished version
dc.contributor.departmentDepartment of Chemistry, activities
uef.solecris.id54395329en
dc.type.publicationTieteelliset aikakauslehtiartikkelit
dc.rights.accessrights© Authors
dc.relation.doi10.1371/journal.pone.0196691
dc.description.reviewstatuspeerReviewed
dc.format.pagerangee0196691
dc.relation.issn1932-6203
dc.relation.issue5
dc.relation.volume13
dc.rights.accesslevelopenAccess
dc.type.okmA1
uef.solecris.openaccessOpen access -julkaisukanavassa ilmestynyt julkaisu


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record