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Borate as a synergistic anion for Marinobacter algicola ferric binding protein, FbpA: a role for boron in iron transport in marine life.

Publication ,  Journal Article
Weerasinghe, AJ; Amin, SA; Barker, RA; Othman, T; Romano, AN; Parker Siburt, CJ; Tisnado, J; Lambert, LA; Huxford, T; Carrano, CJ; Crumbliss, AL
Published in: Journal of the American Chemical Society
October 2013

Boron in the ocean is generally considered a nonbiological element due to its relatively high concentration (0.4 mM) and depth independent concentration profile. Here we report an unexpected role for boron in the iron transport system of the marine bacterium Marinobacter algicola. Proteome analysis under varying boron concentrations revealed that the periplasmic ferric binding protein (Mb-FbpA) was among the proteins whose expression was most affected, strongly implicating the involvement of boron in iron utilization. Here we show that boron facilitates Fe(3+) sequestration by Mb-FbpA at pH 8 (oceanic pH) by acting as a synergistic anion (B(OH)4(1-)). Fe(3+) sequestration does not occur at pH 6.5 where boric acid (B(OH)3; pK(a) = 8.55) is the predominant species. Borate anion is also shown to bind to apo-Mb-FbpA with mM affinity at pH 8, consistent with the biological relevance implied from boron's oceanic concentration (0.4 mM). Borate is among those synergistic anions tested which support the strongest Fe(3+) binding to Mb-FbpA, where the range of anion dependent affinity constants is log K'(eff) = 21-22. Since the pKa of boric acid (8.55) lies near the pH of ocean water, changes in oceanic pH, as a consequence of fluctuations in atmospheric CO2, may perturb iron uptake in many marine heterotrophic bacteria due to a decrease in oceanic borate anion concentration.

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Published In

Journal of the American Chemical Society

DOI

EISSN

1520-5126

ISSN

0002-7863

Publication Date

October 2013

Volume

135

Issue

39

Start / End Page

14504 / 14507

Related Subject Headings

  • Models, Molecular
  • Marinobacter
  • Iron-Binding Proteins
  • Iron
  • General Chemistry
  • Boron
  • Borates
  • Bacterial Proteins
  • Anions
  • 40 Engineering
 

Citation

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Weerasinghe, A. J., Amin, S. A., Barker, R. A., Othman, T., Romano, A. N., Parker Siburt, C. J., … Crumbliss, A. L. (2013). Borate as a synergistic anion for Marinobacter algicola ferric binding protein, FbpA: a role for boron in iron transport in marine life. Journal of the American Chemical Society, 135(39), 14504–14507. https://doi.org/10.1021/ja406609s
Weerasinghe, Aruna J., Shady A. Amin, Ryan A. Barker, Thaer Othman, Ariel N. Romano, Claire J. Parker Siburt, Jerrell Tisnado, et al. “Borate as a synergistic anion for Marinobacter algicola ferric binding protein, FbpA: a role for boron in iron transport in marine life.Journal of the American Chemical Society 135, no. 39 (October 2013): 14504–7. https://doi.org/10.1021/ja406609s.
Weerasinghe AJ, Amin SA, Barker RA, Othman T, Romano AN, Parker Siburt CJ, et al. Borate as a synergistic anion for Marinobacter algicola ferric binding protein, FbpA: a role for boron in iron transport in marine life. Journal of the American Chemical Society. 2013 Oct;135(39):14504–7.
Weerasinghe, Aruna J., et al. “Borate as a synergistic anion for Marinobacter algicola ferric binding protein, FbpA: a role for boron in iron transport in marine life.Journal of the American Chemical Society, vol. 135, no. 39, Oct. 2013, pp. 14504–07. Epmc, doi:10.1021/ja406609s.
Weerasinghe AJ, Amin SA, Barker RA, Othman T, Romano AN, Parker Siburt CJ, Tisnado J, Lambert LA, Huxford T, Carrano CJ, Crumbliss AL. Borate as a synergistic anion for Marinobacter algicola ferric binding protein, FbpA: a role for boron in iron transport in marine life. Journal of the American Chemical Society. 2013 Oct;135(39):14504–14507.
Journal cover image

Published In

Journal of the American Chemical Society

DOI

EISSN

1520-5126

ISSN

0002-7863

Publication Date

October 2013

Volume

135

Issue

39

Start / End Page

14504 / 14507

Related Subject Headings

  • Models, Molecular
  • Marinobacter
  • Iron-Binding Proteins
  • Iron
  • General Chemistry
  • Boron
  • Borates
  • Bacterial Proteins
  • Anions
  • 40 Engineering