Engineered chimeras reveal the structural basis of hexacoordination in globins: A case study of neuroglobin and myoglobin

dc.creatorBoron, Carlos Ignacio
dc.creatorCapece, Luciana
dc.creatorPennacchietti, Francesca
dc.creatorWetzler, Diana Elena
dc.creatorBruno, Stefano
dc.creatorAbbruzzetti, Stefania
dc.creatorChisari, Lucía
dc.creatorLuque, F. Javier
dc.creatorViappiani, Cristiano
dc.creatorMarti, Marcelo Adrian
dc.creatorEstrin, Dario Ariel
dc.creatorNadra, Alejandro Daniel
dc.date.accessioned2021-02-17T12:17:13Z
dc.date.accessioned2022-10-14T22:46:04Z
dc.date.available2021-02-17T12:17:13Z
dc.date.available2022-10-14T22:46:04Z
dc.date.created2021-02-17T12:17:13Z
dc.date.issued2014-10
dc.identifierBoron, Carlos Ignacio; Capece, Luciana; Pennacchietti, Francesca; Wetzler, Diana Elena; Bruno, Stefano; et al.; Engineered chimeras reveal the structural basis of hexacoordination in globins: A case study of neuroglobin and myoglobin; Elsevier Science; Biochimica et Biophysica Acta - General Subjects; 1850; 1; 10-2014; 169-177
dc.identifier0304-4165
dc.identifierhttp://hdl.handle.net/11336/125773
dc.identifierCONICET Digital
dc.identifierCONICET
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/4315604
dc.description.abstractBackground Myoglobin (Mb) and neuroglobin (Ngb) are representative members of pentacoordinated and bis-histidyl, hexacoordinated globins. In spite of their low sequence identity, they show surprisingly similar three-dimensional folds. The ability of Ngb to form a hexacoordinated bis-histidyl complex with the distal HisE7 has a strong impact on ligand affinity. The factors governing such different behaviors have not been completely understood yet, even though they are extremely relevant to establish structure-function relationships within the globin superfamily.
dc.languageeng
dc.publisherElsevier Science
dc.relationinfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0304416514003420
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.bbagen.2014.10.006
dc.rightshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectBIS-HISTIDYL COORDINATION
dc.subjectFLASH PHOTOLYSIS
dc.subjectMOLECULAR DYNAMICS
dc.subjectMYOGLOBIN
dc.subjectNEUROGLOBIN
dc.titleEngineered chimeras reveal the structural basis of hexacoordination in globins: A case study of neuroglobin and myoglobin
dc.typeinfo:eu-repo/semantics/article
dc.typeinfo:ar-repo/semantics/artículo
dc.typeinfo:eu-repo/semantics/publishedVersion


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