Ferric ion (hydr)oxo clusters in the “Venus flytrap” cleft of FbpA: Mössbauer, calorimetric and mass spectrometric studies
作者： Arindam Mukherjee , Paul R. Bilton , Logan Mackay , Adam Janoschka , Haizhong Zhu
DOI: 10.1007/S00775-012-0878-Z
关键词: Fourier transform ion cyclotron resonance 、 Escherichia coli 、 Isothermal titration calorimetry 、 Crystallography 、 Mutant 、 Binding protein 、 Chemistry 、 Mössbauer spectroscopy 、 Binding constant 、 Cluster (physics) 、 Inorganic chemistry
摘要: Isothermal calorimetric studies of the binding iron(III) citrate to ferric ion protein from Neisseria gonorrhoeae suggested complexation a tetranuclear cluster as single step event (apparent constant K appITC = 6.0(5) × 105 M−1). High-resolution Fourier transform cyclotron resonance mass spectrometric data supported oxo(hydroxo) formula [Fe4O2(OH)4(H2O)(cit)]+ in interdomain cleft FbpA. The mutant H9Y-nFbpA showed twofold increase apparent [K 1.1(7) 106 M−1] for compared wild-type protein. Mossbauer spectra Escherichia coli cells overexpressing FbpA and cultured presence added 57Fe were indicative dinuclear polynuclear clusters. therefore appears have strong affinity iron clusters iron-rich environments, property which might endow with new biological functions.
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