Highly malleable haem-binding site of the haemoprotein HasA permits stable accommodation of bulky tetraphenylporphycenes

Iron(iii)- and cobalt(iii)-9,10,19,20-tetraphenylporphycenes, which possess bulky phenyl groups at the four meso positions of porphycene, were successfully incorporated into the haem acquisition protein HasA secreted by Pseudomonas aeruginosa. Crystal structure analysis revealed that loops surroundi...

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Detalles Bibliográficos
Autores principales: Sakakibara, Erika, Shisaka, Yuma, Onoda, Hiroki, Koga, Daiki, Xu, Ning, Ono, Toshikazu, Hisaeda, Yoshio, Sugimoto, Hiroshi, Shiro, Yoshitsugu, Watanabe, Yoshihito, Shoji, Osami
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society of Chemistry 2019
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9064734/
https://www.ncbi.nlm.nih.gov/pubmed/35515244
http://dx.doi.org/10.1039/c9ra02872b
Descripción
Sumario:Iron(iii)- and cobalt(iii)-9,10,19,20-tetraphenylporphycenes, which possess bulky phenyl groups at the four meso positions of porphycene, were successfully incorporated into the haem acquisition protein HasA secreted by Pseudomonas aeruginosa. Crystal structure analysis revealed that loops surrounding the haem-binding site are highly flexible, remodelling themselves to accommodate bulky metal complexes with significantly different structures from the native haem cofactor.

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