Niobium Uptake and Release by Bacterial Ferric Ion Binding Protein
Ferric ion binding proteins (Fbps) transport FeIII 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)...
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| Published in | Bioinorganic Chemistry and Applications Vol. 2010; no. 1; pp. 68 - 78 |
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| Main Authors | , , , |
| Format | Journal Article |
| Language | English |
| Published |
Egypt
Hindawi Limiteds
01.01.2010
Hindawi Publishing Corporation Hindawi Limited Wiley |
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| Abstract | Ferric ion binding proteins (Fbps) transport FeIII 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 NbV 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 NbV binds strongly to Fbp and that a dinuclear NbV 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. |
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| AbstractList | Ferric ion binding proteins (Fbps) transport FeIII 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 NbV 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 NbV binds strongly to Fbp and that a dinuclear NbV 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. Ferric ion binding proteins (Fbps) transport Fe III 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 Nb V 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 Nb V binds strongly to Fbp and that a dinuclear Nb V 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. Ferric ion binding proteins (Fbps) transport Fe(III) 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 Nb(V) 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 Nb(V) binds strongly to Fbp and that a dinuclear Nb(V) 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. |
| Author | Dominic Campopiano Peter J. Sadler Ian Harvey Yanbo Shi |
| AuthorAffiliation | 3 Department of Chemistry, University of Warwick, Coventry CV4 7AL, UK 2 CLRC Daresbury Laboratory, Warrington WA4 4AD, UK 1 School of Chemistry, University of Edinburgh, King's Buildings, West Mains Road, Edinburgh EH9 3JJ, UK |
| AuthorAffiliation_xml | – name: 3 Department of Chemistry, University of Warwick, Coventry CV4 7AL, UK – name: 1 School of Chemistry, University of Edinburgh, King's Buildings, West Mains Road, Edinburgh EH9 3JJ, UK – name: 2 CLRC Daresbury Laboratory, Warrington WA4 4AD, UK |
| Author_xml | – sequence: 1 givenname: Yanbo surname: Shi fullname: Shi, Yanbo organization: School of ChemistryUniversity of EdinburghKing's Buildings, West Mains RoadEdinburgh EH9 3JJUKed.ac.uk – sequence: 2 givenname: Ian surname: Harvey fullname: Harvey, Ian organization: CLRC Daresbury LaboratoryWarrington WA4 4ADUKdl.ac.uk – sequence: 3 givenname: Dominic surname: Campopiano fullname: Campopiano, Dominic organization: School of ChemistryUniversity of EdinburghKing's Buildings, West Mains RoadEdinburgh EH9 3JJUKed.ac.uk – sequence: 4 givenname: Peter J. surname: Sadler fullname: Sadler, Peter J. organization: Department of ChemistryUniversity of WarwickCoventry CV4 7ALUKwarwick.ac.uk |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/20445753$$D View this record in MEDLINE/PubMed |
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| CitedBy_id | crossref_primary_10_1016_j_bbagen_2011_06_019 crossref_primary_10_1016_j_bbagen_2011_09_001 crossref_primary_10_1039_C8DT01145A crossref_primary_10_1186_s11671_020_03375_0 crossref_primary_10_1016_j_jinorgbio_2011_10_010 |
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| ContentType | Journal Article |
| Copyright | Copyright © 2010 Copyright © 2010 Yanbo Shi et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Copyright © 2010 Yanbo Shi et al. 2010 |
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| Snippet | Ferric ion binding proteins (Fbps) transport FeIII across the periplasm and are vital for the virulence of many Gram negative bacteria. Iron(III) is tightly... Ferric ion binding proteins (Fbps) transport Fe(III) across the periplasm and are vital for the virulence of many Gram negative bacteria. Iron(III) is tightly... Ferric ion binding proteins (Fbps) transport Fe III across the periplasm and are vital for the virulence of many Gram negative bacteria. Iron(III) is tightly... Ferric ion binding proteins (Fbps) transport Fe III across the periplasm and are vital for the virulence of many Gram negative bacteria. Iron(III) is tightly... |
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| SubjectTerms | Anions Antibiotics Aqueous solutions Bacteria Binding Biological Colleges & universities Drug resistance E coli Mass spectrometry Neisseria gonorrhoeae Niobium Phosphates Proteins Uptakes |
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| Title | Niobium Uptake and Release by Bacterial Ferric Ion Binding Protein |
| URI | https://www.airitilibrary.com/Article/Detail/P20160523001-201012-201704070005-201704070005-68-78 https://dx.doi.org/10.1155/2010/307578 https://www.ncbi.nlm.nih.gov/pubmed/20445753 https://www.proquest.com/docview/855580803 https://search.proquest.com/docview/1671385088 https://search.proquest.com/docview/733356088 https://search.proquest.com/docview/744691952 https://pubmed.ncbi.nlm.nih.gov/PMC2860717 https://doaj.org/article/02c0a8a984c9419aa71046ea0efe9a7a |
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