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

Erika SakakibaraYuma ShisakaHiroki OnodaDaiki KogaNing XuToshikazu OnoYoshio HisaedaHiroshi SugimotoYoshitsugu ShiroYoshihito WatanabeOsami Shoji
Published in: RSC advances (2019)
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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