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


ABSTRACT: 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.

SUBMITTER: Sakakibara E 

PROVIDER: S-EPMC9064734 | biostudies-literature | 2019 Jun

REPOSITORIES: biostudies-literature

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

Sakakibara Erika E   Shisaka Yuma Y   Onoda Hiroki H   Koga Daiki D   Xu Ning N   Ono Toshikazu T   Hisaeda Yoshio Y   Sugimoto Hiroshi H   Shiro Yoshitsugu Y   Watanabe Yoshihito Y   Shoji Osami O  

RSC advances 20190613 32


Iron(iii)- and cobalt(iii)-9,10,19,20-tetraphenylporphycenes, which possess bulky phenyl groups at the four <i>meso</i> positions of porphycene, were successfully incorporated into the haem acquisition protein HasA secreted by <i>Pseudomonas aeruginosa</i>. 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. ...[more]

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