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Structures of the Heme Acquisition Protein HasA with Iron(III)-5,15-Diphenylporphyrin and Derivatives Thereof as an Artificial Prosthetic Group.

Uehara H, Shisaka Y, Nishimura T, Sugimoto H, Shiro Y, Miyake Y, Shinokubo H, Watanabe Y, Shoji O
Angew Chem Int Ed Engl 56 15279-15283 (2017)
Related entries: 5xa4, 5xic, 5xie, 5xkb

Cited: 5 times
EuropePMC logo PMID: 28921809

Abstract

Iron(III)-5,15-diphenylporphyrin and several derivatives were accommodated by HasA, a heme acquisition protein 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 the 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.

Reviews citing this publication (3)

  1. Pseudomonas aeruginosa: pathogenesis, virulence factors, antibiotic resistance, interaction with host, technology advances and emerging therapeutics. Qin S, Xiao W, Zhou C, Pu Q, Deng X, Lan L, Liang H, Song X, Wu M. Signal Transduct Target Ther 7 199 (2022)
  2. Metallotherapeutics development in the age of iron-clad bacteria. Centola G, Xue F, Wilks A. Metallomics 12 1863-1877 (2020)
  3. A zero-sum game or an interactive frame? Iron competition between bacteria and humans in infection war. Wu Z, Shao J, Zheng J, Liu B, Li Z, Shen N. Chin Med J (Engl) 135 1917-1926 (2022)

Articles citing this publication (2)

  1. Corrole-Substituted Fluorescent Heme Proteins. Lemon CM, Marletta MA. Inorg Chem 60 2716-2729 (2021)
  2. Highly malleable haem-binding site of the haemoprotein HasA permits stable accommodation of bulky tetraphenylporphycenes. Sakakibara E, Shisaka Y, Onoda H, Koga D, Xu N, Ono T, Hisaeda Y, Sugimoto H, Shiro Y, Watanabe Y, Shoji O. RSC Adv 9 18697-18702 (2019)


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