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- W2014189869 abstract "Although the presence of an exogenous anion is a requirement for tight Fe 3+ binding by the bacterial ( Neisseria ) transferrin n Fbp, the identity of the exogenous anion is not specific in vitro. n Fbp was reconstituted as a stable iron containing protein by using a number of different exogenous anions [arsenate, citrate, nitrilotriacetate, pyrophosphate, and oxalate (symbolized by X)] in addition to phosphate, predominantly present in the recombinant form of the protein. Spectroscopic characterization of the Fe 3+ /anion interaction in the reconstituted protein was accomplished by UV-visible and EPR spectroscopies. The affinity of the protein for Fe 3+ is anion dependent, as evidenced by the effective Fe 3+ binding constants ( K ′ eff ) observed, which range from 1 × 10 17 M −1 to 4 × 10 18 M −1 at pH 6.5 and 20°C. The redox potentials for Fe 3+ n FbpX/Fe 2+ n FbpX reduction are also found to depend on the identity of the synergistic anion required for Fe 3+ sequestration. Facile exchange of exogenous anions (Fe 3+ n FbpX + X′ → Fe 3+ n FbpX′ + X) is established and provides a pathway for environmental modulation of the iron chelation and redox characteristics of n Fbp. The affinity of the iron loaded protein for exogenous anion binding at pH 6.5 was found to decrease in the order phosphate > arsenate ∼ pyrophosphate > nitrilotriacetate > citrate ∼ oxalate ≫ carbonate. Anion influence on the iron primary coordination sphere through iron binding and redox potential modulation may have in vivo application as a mechanism for periplasmic control of iron delivery to the cytosol." @default.
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- W2014189869 date "2003-03-19" @default.
- W2014189869 modified "2023-10-15" @default.
- W2014189869 title "The influence of the synergistic anion on iron chelation by ferric binding protein, a bacterial transferrin" @default.
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- W2014189869 doi "https://doi.org/10.1073/pnas.0536897100" @default.
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