Inhibition of Heme Uptake in Pseudomonas aeruginosa by its Hemophore (HasAp) Bound to Synthetic Metal Complexes

The heme acquisition system A protein secreted by Pseudomonas aeruginosa (HasAp) can capture several synthetic metal complexes other than heme. The crystal structures of HasAp harboring synthetic metal complexes revealed only small perturbation of the overall HasAp structure. An inhibitory effect up...

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Published inAngewandte Chemie Vol. 126; no. 11; pp. 2906 - 2910
Main Authors Shirataki, Chikako, Shoji, Osami, Terada, Mitsuyoshi, Ozaki, Shin-ichi, Sugimoto, Hiroshi, Shiro, Yoshitsugu, Watanabe, Yoshihito
Format Journal Article
LanguageEnglish
Published Weinheim WILEY-VCH Verlag 10.03.2014
WILEY‐VCH Verlag
Wiley Subscription Services, Inc
Subjects
Acquisitions
Chemistry
Crystal structure
Eisenkomplexe
HasA
Häm-Proteine
Iron
Marketing
Metals
Monitoring
Proteinstrukturen
Pseudomonas aeruginosa
Synthetic metals
Uptakes
Wachstumshemmer
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Summary:The heme acquisition system A protein secreted by Pseudomonas aeruginosa (HasAp) can capture several synthetic metal complexes other than heme. The crystal structures of HasAp harboring synthetic metal complexes revealed only small perturbation of the overall HasAp structure. An inhibitory effect upon heme acquisition by HasAp bearing synthetic metal complexes was examined by monitoring the growth of Pseudomonas aeruginosa PAO1. HasAp bound to iron–phthalocyanine inhibits heme acquisition in the presence of heme‐bound HasAp as an iron source. Konkurrenz für Häm‐Komplexe: Der Hämophor HasAp aus Pseudomonas aeruginosa bindet viele synthetische Metallkomplexe, so auch Fe‐Salophen (gelb), Fe‐Phthalocyanin (Fe‐Pc; türkis) und Fe‐Mesoporphyrin IX (rosa). Die Kristallstrukturen von HasAp in Kombination mit diesen Metallkomplexen zeigen kleine Strukturänderungen im Vergleich zu Häm‐beladenem HasAp. Fe‐Pc‐HasAp inhibiert die HasAp‐vermittelte Häm‐Aufnahme durch P. aeruginosa.
Bibliography:MEXT
Ministry of Education, Culture, Sports, Science, and Technology
ArticleID:ANGE201307889
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This work was supported by Grants-in-Aid for Scientific Research (S) to Y. W. (24225004), Grant-in-Aid for Scientific Research on Innovative Areas "Molecular Activation Directed toward Straightforward Synthesis" to Y. S. (22105012) and to O. S. (25105724), and a Grant-in-Aid for Young Scientists (A) to O.S. (21685018) from the Ministry of Education, Culture, Sports, Science, and Technology (MEXT) (Japan). C.S. was supported by Global COE Program "Elucidation and Design of Materials and Molecular Functions" and the Program for Leading Graduate Schools "Integrative Graduate Education and Research Program in Green Natural Sciences" by MEXT (Japan). We thank Dr. Go Ueno, Dr. Yuki Nakamura, Dr. Hironori Murakami, and Dr. Nobuyuki Shimizu for their assistance with the data collection at SPring-8.
This work was supported by Grants‐in‐Aid for Scientific Research (S) to Y. W. (24225004), Grant‐in‐Aid for Scientific Research on Innovative Areas “Molecular Activation Directed toward Straightforward Synthesis” to Y. S. (22105012) and to O. S. (25105724), and a Grant‐in‐Aid for Young Scientists (A) to O.S. (21685018) from the Ministry of Education, Culture, Sports, Science, and Technology (MEXT) (Japan). C.S. was supported by Global COE Program “Elucidation and Design of Materials and Molecular Functions” and the Program for Leading Graduate Schools “Integrative Graduate Education and Research Program in Green Natural Sciences” by MEXT (Japan). We thank Dr. Go Ueno, Dr. Yuki Nakamura, Dr. Hironori Murakami, and Dr. Nobuyuki Shimizu for their assistance with the data collection at SPring‐8.
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SourceType-Scholarly Journals-1
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ISSN:0044-8249
1521-3757
DOI:10.1002/ange.201307889