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

Erika Sakakibara, Yuma Shisaka, Hiroki Onoda, Daiki Koga, Ning Xu, Toshikazu Ono, Yoshio Hisaeda, Hiroshi Sugimoto, Yoshitsugu Shiro, Yoshihito Watanabe, Osami Shoji

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)18697-18702
Number of pages6
JournalRSC Advances
Volume9
Issue number32
DOIs
Publication statusPublished - 2019

All Science Journal Classification (ASJC) codes

  • Chemistry(all)
  • Chemical Engineering(all)

Fingerprint Dive into the research topics of 'Highly malleable haem-binding site of the haemoprotein HasA permits stable accommodation of bulky tetraphenylporphycenes'. Together they form a unique fingerprint.

Cite this