Phosphate ester hydrolysis is catalyzed by a bacterial transferrin: potential implications for in vivo iron transport mechanisms
Author:
Publisher
Elsevier BV
Subject
Inorganic Chemistry,Biochemistry
Reference14 articles.
1. Structural Biology of Bacterial Iron Uptake Systems
2. Fe3+ Coordination and Redox Properties of a Bacterial Transferrin
3. The influence of the synergistic anion on iron chelation by ferric binding protein, a bacterial transferrin
4. Synergistic Anion and Metal Binding to the Ferric Ion-binding Protein from Neisseria gonorrhoeae
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1. Complexation modulated redox behavior of transition metal systems (review);Russian Journal of General Chemistry;2015-04
2. The Study of the Hydrolysis of the Phosphate Diester Catalyzed by an Anion Metallomicelle of Ce3+-Diethylenetriamine;Advanced Materials Research;2012-07
3. FbpA — A bacterial transferrin with more to offer;Biochimica et Biophysica Acta (BBA) - General Subjects;2012-03
4. Uptake and release of metal ions by transferrin and interaction with receptor 1;Biochimica et Biophysica Acta (BBA) - General Subjects;2012-03
5. Ferric ion (hydr)oxo clusters in the “Venus flytrap” cleft of FbpA: Mössbauer, calorimetric and mass spectrometric studies;JBIC Journal of Biological Inorganic Chemistry;2012-02-17
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