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- W2170804940 abstract "Ferric ion binding proteins (Fbps) transport<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mrow><mml:msup><mml:mrow><mml:mtext>Fe</mml:mtext></mml:mrow><mml:mrow><mml:mtext>III</mml:mtext></mml:mrow></mml:msup></mml:mrow></mml:math>across the periplasm and are vital for the virulence of many Gram negative bacteria. Iron(III) is tightly bound in a hinged binding cleft with octahedral coordination geometry involving binding to protein side chains (including tyrosinate residues) together with a synergistic anion such as phosphate. Niobium compounds are of interest for their potential biological activity, which has been little explored. We have studied the binding of cyclopentadienyl and nitrilotriacetato<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mrow><mml:msup><mml:mrow><mml:mtext>Nb</mml:mtext></mml:mrow><mml:mtext>V</mml:mtext></mml:msup></mml:mrow></mml:math>complexes to the Fbp from Neisseria gonorrhoeae by UV-vis spectroscopy, chromatography, ICP-OES, mass spectrometry, and Nb K-edge X-ray absorption spectroscopy. These data suggest that<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mrow><mml:msup><mml:mrow><mml:mtext>Nb</mml:mtext></mml:mrow><mml:mtext>V</mml:mtext></mml:msup></mml:mrow></mml:math>binds strongly to Fbp and that a dinuclear<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML><mml:mrow><mml:msup><mml:mrow><mml:mtext>Nb</mml:mtext></mml:mrow><mml:mtext>V</mml:mtext></mml:msup></mml:mrow></mml:math>centre can be readily accommodated in the interdomain binding cleft. The possibility of designing niobium-based antibiotics which block iron uptake by pathogenic bacteria is discussed." @default.
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- W2170804940 date "2010-01-01" @default.
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- W2170804940 title "Niobium Uptake and Release by Bacterial Ferric Ion Binding Protein" @default.
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- W2170804940 doi "https://doi.org/10.1155/2010/307578" @default.
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