Journal
CHEMBIOCHEM
Volume 23, Issue 14, Pages -Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.202200095
Keywords
drug delivery; heme proteins; protein structures; Pseudomonas aeruginosa; tetraphenylporphyrin
Funding
- JSPS KAKENHI [JP15H05806, JP18H02084, JP18J15250, JP21J15614, JP18J23340]
- JST CREST [JPMJCR15P3]
- SUNBOR scholarship from the SUNTORY FOUNDATION for LIFE SCIENCES
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A stable complex between HasA and TPP was reported, which can inhibit the growth of Pseudomonas aeruginosa and mutant variants of HasA binding FeTPP show a different coordination mode that allows the cyclopropanation of styrene.
Tetraphenylporphyrin (TPP) is a symmetrically substituted synthetic porphyrin whose properties can be readily modified, providing it with significant advantages over naturally occurring porphyrins. Herein, we report the first example of a stable complex between a native biomolecule, the haemoprotein HasA, and TPP as well as its derivatives. The X-ray crystal structures of nine different HasA-TPP complexes were solved at high resolutions. HasA capturing TPP derivatives was also demonstrated to inhibit growth of the opportunistic pathogen Pseudomonas aeruginosa. Mutant variants of HasA binding FeTPP were shown to possess a different mode of coordination, permitting the cyclopropanation of styrene.
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