Construction and Crystal Structure Analysis of Heme Acquisition Protein HasA Containing Iron(III)-5,15-Diphenylporphyrin and Derivatives Thereof as an Artificial Prosthetic Group
 

Construction and Crystal Structure Analysis of Heme Acquisition Protein HasA Containing Iron(III)-5,15-Diphenylporphyrin and Derivatives Thereof as an Artificial Prosthetic Group


Iron(III)-5,15-diphenylporphyrin (1) and its derivatives (2-7) were accommodated by the heme acquisition protein HasA secreted by Pseudomonas aeruginosa, despite possessing bulky substituents at the meso-position of the porphyrin. Crystal structure analysis revealed that the two phenyl groups at the meso-positions of porphyrin extend outside HasA. It was shown that growth of P. aeruginosa was inhibited in the presence of HasA coordinating the synthetic porphyrins under iron-limiting conditions, and that the structure of the synthetic porphyrins greatly affects the inhibition efficiency.

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