A soft X-ray synchrotron study of the charge state of iron ions in the ferrihydrite core of the ferritin Dps protein in Escherichia coli

The Escherichia coli Dps protein belongs to a specific family of bacterial ferritins; it is a nanosized particle that contains an inorganic core (~5 nm in diameter) and a protein shell with a size of 8–9 nm. The protein shell consists of 12 identical subunits with the known crystal structure of a dodecamer. The composition and structure of the core have been less studied. The core formation is associated with the oxidation products of Fe2+ ions in the ferroxidase centers of the protein. Thus, Fe2O3 oxides are the main compounds of the core. However, the mineralization properties of Fe2+ ions under anaerobic conditions in vitro may indicate a more complicated composition of the core in the native Dps protein. This paper presents a technique for the preparation of purified Dps samples for ultrahigh vacuum synchrotron experiments by X-ray absorption near edge structure spectroscopy of the iron absorption edge in the soft X-ray region. The conducted synchrotron experiments have revealed the presence of both trivalent and divalent iron ions in the octahedral and tetrahedral environment of oxygen atoms in the prepared biological samples. This points to a complex ionic composition of the core even in the native Dps protein, which has been isolated from aerobically grown bacteria.