Borate as a Synergistic Anion for Marinobacter algicola Ferric Binding Protein, FbpA: A Role for Boron in Iron Transport in Marine Life

2013 ◽  
Vol 135 (39) ◽  
pp. 14504-14507 ◽  
Author(s):  
Aruna J. Weerasinghe ◽  
Shady A. Amin ◽  
Ryan A. Barker ◽  
Thaer Othman ◽  
Ariel N. Romano ◽  
...  
Keyword(s):  
Iron Transport ◽  
Binding Protein ◽  
Marine Life ◽  
Ferric Binding Protein

scholarly journals Anion-independent Iron Coordination by the Campylobacter jejuni Ferric Binding Protein

2005 ◽  
Vol 280 (10) ◽  
pp. 9283-9290 ◽  
Author(s):  
Stacey A.L. Tom-Yew ◽  
Diana T. Cui ◽  
Elena G. Bekker ◽  
Michael E.P. Murphy
Keyword(s):  
Campylobacter Jejuni ◽  
Binding Protein ◽  
Ferric Binding Protein ◽  
Iron Coordination

SUPREX (Stability of Unpurified Proteins from Rates of H/D Exchange) Analysis of the Thermodynamics of Synergistic Anion Binding by Ferric-Binding Protein (FbpA), a Bacterial Transferrin†

Biochemistry ◽  
2004 ◽  
Vol 43 (50) ◽  
pp. 15767-15774 ◽  
Author(s):  
Petra L. Roulhac ◽  
Kendall D. Powell ◽  
Suraj Dhungana ◽  
Katherine D. Weaver ◽  
Timothy A. Mietzner ◽  
...  
Keyword(s):  
Binding Protein ◽  
Anion Binding ◽  
Ferric Binding Protein ◽  
Bacterial Transferrin

scholarly journals The influence of the synergistic anion on iron chelation by ferric binding protein, a bacterial transferrin

2003 ◽  
Vol 100 (7) ◽  
pp. 3659-3664 ◽  
Author(s):  
S. Dhungana ◽  
C. H. Taboy ◽  
D. S. Anderson ◽  
K. G. Vaughan ◽  
P. Aisen ◽  
...  
Keyword(s):  
Binding Protein ◽  
Protein A ◽  
Iron Chelation ◽  
Ferric Binding Protein ◽  
Bacterial Transferrin

scholarly journals Characterization of a ferric‐binding protein mutant in Haemophilus influenzae

1997 ◽  
Vol 25 (5) ◽  
pp. 979-987 ◽  
Author(s):  
Shane D. Kirby ◽  
Scott D. Gray‐Owen ◽  
Anthony B. Schryvers
Keyword(s):  
Haemophilus Influenzae ◽  
Binding Protein ◽  
Ferric Binding Protein

scholarly journals Pulsed ELDOR Measurement of the Distance Between a Spin-Label and Copper (II) Centre in the Copper Loaded R48C Mutant of N. gonorrhoeae Ferric Binding Protein

2018 ◽  
Author(s):  
Matt Bawn ◽  
Justin Bradley ◽  
Fraser MacMillan
Keyword(s):  
Spin Label ◽  
Binding Protein ◽  
Double Resonance ◽  
Distance Measurements ◽  
Paramagnetic Resonance ◽  
Distance Determination ◽  
Pulsed Epr ◽  
Ferric Binding Protein ◽  
Relaxation Experiments ◽  
Electron Paramagnetic

AbstractDistance determination in proteins and biomolecules using pulsed EPR (electron paramagnetic resonance) techniques is becoming an increasingly popular and accessible technique. PELDOR (pulsed electron-electron double resonance), is a technique designed for distance determination over a nanoscopic scale. Here, ferric binding protein (Fbp) is used to demonstrate the practicability of this technique to Cu (II) Metalloproteins. PELDOR is usually applied to bi-radicals or endogenous radicals, and distance determination using pulsed EPR of metal containing centres in biomolecules has been restricted to relaxation experiments. PELDOR distance measurements between a Cu (II) ion and a nitroxide have previously only been reported for model compounds [1, 2].Fbp as the name suggests usually, contains a Fe (III) ion centre. For the purposes of this investigation the Fe (III) ion was removed and replaced by a Cu (II) ion, after a nitroxide spin-label was added to the Fbp using of site directed spin-labelling (SDSL). PELDOR was then applied to measure the distance between the two centres.Simulation methods were then employed to fully investigate these data and allow a quantitative interpretation of the copper nitroxide PELDOR data. The observed PELDOR time traces were analysed using DEER analysis[3].

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