Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/4032
DC FieldValueLanguage
dc.contributor.authorI., Bertinien_us
dc.contributor.authorF., Brigantien_us
dc.contributor.authorMangani, Stefanoen_us
dc.contributor.authorH. F., Noltingen_us
dc.contributor.authorA., Scozzafavaen_us
dc.date.accessioned2021-03-30T14:41:15Z-
dc.date.available2021-03-30T14:41:15Z-
dc.date.issued1994-
dc.identifier.issn0014-5793en_US
dc.identifier.urihttp://hdl.handle.net/20.500.12779/4032-
dc.description47983en_US
dc.description.abstractThe interactions of catechol (substrate), 2-hydroxy-pyridine-N-oxide (substrate analogue), and 2-bromophenol (inhibitor) with the extradiol cleaving catechol-2,3-dioxygenase from Pseudomonas putida mt-2 have been monitored through X-ray absorption spectroscopy (XAS). The analysis of the data provides details about the mode of coordination of the substrate and of the inhibitors to the active site of the enzyme.en_US
dc.language.isoenen_US
dc.relationNoneen_US
dc.relation.ispartofFEBS LETTERSen_US
dc.subjectEXAFS, catchol dioxygenase; ironen_US
dc.titleSubstrate, Substrate-analog, and Inhibitor Interactions With the Ferrous Active-site of Catechol 2,3-dioxygenase Monitored Through Xas Studiesen_US
dc.typeArticleen_US
dc.identifier.doi10.1016/0014-5793(94)00771-3en_US
dc.identifier.pmid8070565en_US
dc.identifier.scopus2-s2.0-0028041295en_US
dc.identifier.isiWOS:A1994PD82000014en_US
dc.relation.volume350en_US
dc.relation.issue2-3en_US
dc.description.firstpage207en_US
dc.description.lastpage212en_US
dc.description.thirdmissionNot applicableen_US
item.cerifentitytypePublications-
item.grantfulltextnone-
item.languageiso639-1en-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.openairetypeArticle-
item.fulltextNo Fulltext-
crisitem.author.orcid0000-0003-4824-7478-
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