Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/3917
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dc.contributor.authorMangani, Stefanoen_us
dc.contributor.authorK., Hakanssonen_us
dc.date.accessioned2021-03-30T14:36:22Z-
dc.date.available2021-03-30T14:36:22Z-
dc.date.issued1992-
dc.identifier.issn0014-2956en_US
dc.identifier.urihttp://hdl.handle.net/20.500.12779/3917-
dc.description47991en_US
dc.description.abstractThe structures of human carbonic-anhydrase-II complexes with the anionic inhibitors hydrogen sulphide (HS-) and nitrate (NO3-) have been determined by X-ray diffraction at 0.19-nm resolution from crystals soaked at pH 7.8 and 6.0, respectively. The modes of binding of these two anions differ markedly from each other. The strong inhibitor HS- replaces the native zinc-bound water/hydroxide (Wat263) leaving the tetrahedral metal geometry unaltered and acts as a hydrogen-bonding donor towards Thr199gamma. The weak NO3- inhibitor does not displace Wat263 from the metal coordination but occupies a fifth binding site changing the zinc coordination polyhedron into a slightly distorted trigonal bipyramid. The interaction of NO3- with the metal is weak; the nearest of its oxygen atoms being at a distance of 0.28 nm from the zinc ion. The binding of nitrate to the enzyme is completed by a hydrogen bond to the metal coordinated Wat263 and a second one to a water molecule of the active-site cavity. The structures of the two complexes help to rationalize the binding of anionic inhibitors to carbonic anhydrase and the binding mode displayed by NO3- may be relevant to the catalytic mechanism.en_US
dc.language.isoenen_US
dc.relationNoneen_US
dc.relation.ispartofEUROPEAN JOURNAL OF BIOCHEMISTRYen_US
dc.subjectx-ray; crystal structure; human carbonic anhydrase; inhibitoren_US
dc.titleCrystallographic Studies of the Binding of Protonated and Unprotonated Inhibitors To Carbonic-anhydrase Using Hydrogen-sulfide and Nitrate Anionsen_US
dc.typeArticleen_US
dc.identifier.doi10.1111/j.1432-1033.1992.tb17490.xen_US
dc.identifier.pmid1336460en_US
dc.identifier.scopus2-s2.0-0027050732en_US
dc.identifier.isiWOS:A1992KF58100025en_US
dc.relation.volume210en_US
dc.description.firstpage867en_US
dc.description.lastpage871en_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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