Ferric ion (hydr)oxo clusters in the "Venus flytrap" cleft of FbpA: Mössbauer, calorimetric and mass spectrometric studies

Arindam Mukherjee, Paul R Bilton, Logan Mackay, Adam Janoschka, Haizhong Zhu, Dean Rea, Pat R R Langridge-Smith, Dominic J Campopiano, Thomas Teschner, Alfred X Trautwein, Volker Schünemann, Peter J Sadler

Research output: Contribution to journalArticlepeer-review

Abstract

Isothermal calorimetric studies of the binding of iron(III) citrate to ferric ion binding protein from Neisseria gonorrhoeae suggested the complexation of a tetranuclear iron(III) cluster as a single step binding event (apparent binding constant K (app) (ITC)  = 6.0(5) × 10(5) M(-1)). High-resolution Fourier transform ion cyclotron resonance mass spectrometric data supported the binding of a tetranuclear oxo(hydroxo) iron(III) cluster of formula [Fe(4)O(2)(OH)(4)(H(2)O)(cit)](+) in the interdomain binding cleft of FbpA. The mutant H9Y-nFbpA showed a twofold increase in the apparent binding constant [K (app) (ITC)  = 1.1(7) × 10(6) M(-1)] for the tetranuclear iron(III) cluster compared to the wild-type protein. Mössbauer spectra of Escherichia coli cells overexpressing FbpA and cultured in the presence of added (57)Fe citrate were indicative of the presence of dinuclear and polynuclear clusters. FbpA therefore appears to have a strong affinity for iron clusters in iron-rich environments, a property which might endow the protein with new biological functions.
Original languageEnglish
JournalJBIC Journal of Biological Inorganic Chemistry
DOIs
Publication statusPublished - 2012

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