Binding of PDZ domains to the carboxy terminus of inducible nitric oxide synthase boosts electron transfer and NO synthesis

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AudienciaPúblico en generales_ES
CoberturaMéxicoes_ES
Fecha de ingreso2026-09-15T00:31:53Z
Fecha de publicación2015-01-01
ResumeniNOS lacks any phosphorylatable residue at its C‐terminus despite displaying a 25‐residue extension known to block electron transfer and activity. We report that C‐terminal deletions of iNOS increased the cytochrome c reduction rate. Moreover, the interaction of the iNOS C‐terminus with the PDZ domains of EBP50 or CAP70 resulted not only in augmented reductase activity and greater NO synthesis but also anticipated the formation of the air‐stable semiquinone generated after NADPH addition. Hence, the C‐terminus of iNOS regulates the activity of the enzyme, albeit, unlike nNOS and eNOS, displacement of the autoinhibitory element occurs upon binding to proteins with PDZ domains.es_ES
Doihttps://doi.org/10.1016/j.febslet.2015.07.004es_ES
URIhttps://riuat.uat.edu.mx/handle/123456789/3636
Idiomaenes_ES
EditorialWileyes_ES
RelaciónFEBS Letterses_ES
URL relacionadohttps://doi.org/10.1016/j.febslet.2015.07.004es_ES
DerechosAcceso restringido / Suscripción (Metadatos de producción científica)es_ES
Licenciahttp://purl.org/coar/access_right/c_16eces_ES
FuenteFEBS Letters
TítuloBinding of PDZ domains to the carboxy terminus of inducible nitric oxide synthase boosts electron transfer and NO synthesises_ES
TipoArtículoes_ES
ArbitradoHa sido Arbitradoes_ES
AutorAicart-Ramos, Clara
AutorRodríguez-Crespo, Ignacio
AutorAicart-Ramos, Claraes_ES
AutorRodríguez-Crespo, Ignacioes_ES
InstituciónUniversidad Autónoma de Tamaulipas
InstituciónUniversidad Autónoma de Tamaulipases_ES
Número17es_ES
Rango de páginas2207-2212es_ES
URL relacionadahttps://doi.org/10.1016/j.febslet.2015.07.004
Tipo de artículoIndexado
Tipo de artículoIndexadoes_ES
Volumen589es_ES

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