The Coordination Chemistry of Two Peptidic Models of NFeoB and Core CFeoB Regions of FeoB Protein: Complexes of Fe(II), Mn(II), and Zn(II)

Often necessary for efficient Fe(II) trafficking into bacterial cell, the Feo system is a vital transporter for many pathogenic bacteria and indispensable for proper development and survival in the host organism during infection. In this work, we present the metal-binding characteristics of the peptidic models of two putative Fe(II)-binding sites of E. coliFeoB: L1 (Ac-477IMRGEATPFVMELPVYHVPH496-CONH2) being a fragment of the Core CFeoB region located between the transmembrane helices and L2 (Ac-38VERKEG43-CONH2), which represents the ExxE motif found within the NFeoB domain. With a variety of physicochemical methods, such as potentiometry, mass spectrometry, NMR, and EPR spectroscopy, we have determined the stability constants and metal-binding residues for the complexes of Fe(II), Mn(II), and Zn(II) with two ligands, L1 and L2, acting as models for the Core CFeoB and ExxE motif. We compare their affinities toward the studied metal ions with the previously studied C-terminal part of the protein and discuss a possible role in metal trafficking by the whole protein.