4.6 Article

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

Journal

RSC ADVANCES
Volume 9, Issue 32, Pages 18697-18702

Publisher

ROYAL SOC CHEMISTRY
DOI: 10.1039/c9ra02872b

Keywords

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Funding

  1. Ministry of Education, culture, Sports, Science, and Technology [26708018]
  2. Core Research for Evolutional Science and Technology, Japan Science and Technology Agency [JPMJCR15P3]
  3. KAKENHI, Japan Society for the Promotion of Science [JP15H05806, JP18H02084, JP18H04265]
  4. Grants-in-Aid for Scientific Research [26708018] Funding Source: KAKEN

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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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