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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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
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author Sakakibara, Erika
Shisaka, Yuma
Onoda, Hiroki
Koga, Daiki
Xu, Ning
Ono, Toshikazu
Hisaeda, Yoshio
Sugimoto, Hiroshi
Shiro, Yoshitsugu
Watanabe, Yoshihito
Shoji, Osami
author_facet Sakakibara, Erika
Shisaka, Yuma
Onoda, Hiroki
Koga, Daiki
Xu, Ning
Ono, Toshikazu
Hisaeda, Yoshio
Sugimoto, Hiroshi
Shiro, Yoshitsugu
Watanabe, Yoshihito
Shoji, Osami
author_sort Sakakibara, Erika
collection PubMed
description 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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spelling pubmed-90647342022-05-04 Highly malleable haem-binding site of the haemoprotein HasA permits stable accommodation of bulky tetraphenylporphycenes Sakakibara, Erika Shisaka, Yuma Onoda, Hiroki Koga, Daiki Xu, Ning Ono, Toshikazu Hisaeda, Yoshio Sugimoto, Hiroshi Shiro, Yoshitsugu Watanabe, Yoshihito Shoji, Osami RSC Adv Chemistry 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. The Royal Society of Chemistry 2019-06-13 /pmc/articles/PMC9064734/ /pubmed/35515244 http://dx.doi.org/10.1039/c9ra02872b Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by-nc/3.0/
spellingShingle Chemistry
Sakakibara, Erika
Shisaka, Yuma
Onoda, Hiroki
Koga, Daiki
Xu, Ning
Ono, Toshikazu
Hisaeda, Yoshio
Sugimoto, Hiroshi
Shiro, Yoshitsugu
Watanabe, Yoshihito
Shoji, Osami
Highly malleable haem-binding site of the haemoprotein HasA permits stable accommodation of bulky tetraphenylporphycenes
title Highly malleable haem-binding site of the haemoprotein HasA permits stable accommodation of bulky tetraphenylporphycenes
title_full Highly malleable haem-binding site of the haemoprotein HasA permits stable accommodation of bulky tetraphenylporphycenes
title_fullStr Highly malleable haem-binding site of the haemoprotein HasA permits stable accommodation of bulky tetraphenylporphycenes
title_full_unstemmed Highly malleable haem-binding site of the haemoprotein HasA permits stable accommodation of bulky tetraphenylporphycenes
title_short Highly malleable haem-binding site of the haemoprotein HasA permits stable accommodation of bulky tetraphenylporphycenes
title_sort highly malleable haem-binding site of the haemoprotein hasa permits stable accommodation of bulky tetraphenylporphycenes
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9064734/
https://www.ncbi.nlm.nih.gov/pubmed/35515244
http://dx.doi.org/10.1039/c9ra02872b
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