ferrihydrite and hydroxide-ion

In nature or in the laboratory, the roughly spherical interior of the ferritin protein is well suited for the formation and storage of a variety of nanosized metal oxy-hydroxide compounds which hold promise for a range of applications. However, the linkages between ferritin reactivity and the structure and physicochemical properties of the nanoparticle core, either native or reconstituted, remain only partly understood.. Here we review studies, including those from our laboratory, which have investigated the structure of ferritin-derived ferrihydrite and reactivity of ferritin, both native and reconstituted. Selected proposed structure models for ferrihydrite are discussed along with the structural and genetic relationships that exist among several different forms of ferrihydrite. With regard to reactivity, the review will emphasize studies that have investigated the (photo)reactivity of ferritin and ferritin-derived materials with environmentally relevant gaseous and aqueous species.. The inorganic core formed from apoferritin reconstituted with varied amounts of Fe has the same structural topology as the inorganically derived ferrihydrite that is an important component of many environmental and soil systems. Reactivity of ferritin toward aqueous species resulting from the photoexcitation of the inorganic core of the protein shows promise for driving redox reactions relevant to environmental chemistry.. Ferritin-derived ferrihydrite is effectively maintained in a relatively unaggregated state, which improves reactivity and opens the possibility of future applications in environmental remediation. Advances in our understanding of the structure, composition, and disorder in synthetic, inorganically derived ferrihydrite are shedding new light on the reactivity and stability of ferrihydrite derived artificially from ferritin.

Topics: Animals; Ferric Compounds; Ferritins; Humans; Hydroxides; Models, Biological; Models, Molecular; Oxidation-Reduction; Protein Conformation

Ferritin biominerals are protein-caged metabolic iron concentrates used for iron-protein cofactors and oxidant protection (Fe(2+) and O2 sequestration). Fe(2+) passage through ion channels in the protein cages, like membrane ion channels, required for ferritin biomineral synthesis, is followed by Fe(2+) substrate movement to ferritin enzyme (Fox) sites. Fe(2+) and O2 substrates are coupled via a diferric peroxo (DFP) intermediate, λmax 650 nm, which decays to [Fe(3+)-O-Fe(3+)] precursors of caged ferritin biominerals. Structural studies show multiple conformations for conserved, carboxylate residues E136 and E57, which are between ferritin ion channel exits and enzymatic sites, suggesting functional connections. Here we show that E136 and E57 are required for ferritin enzyme activity and thus are functional links between ferritin ion channels and enzymatic sites. DFP formation (Kcat and kcat/Km), DFP decay, and protein-caged hydrated ferric oxide accumulation decreased in ferritin E57A and E136A; saturation required higher Fe(2+) concentrations. Divalent cations (both ion channel and intracage binding) selectively inhibit ferritin enzyme activity (block Fe(2+) access), Mn(2+) << Co(2+) < Cu(2+) < Zn(2+), reflecting metal ion-protein binding stabilities. Fe(2+)-Cys126 binding in ferritin ion channels, observed as Cu(2+)-S-Cys126 charge-transfer bands in ferritin E130D UV-vis spectra and resistance to Cu(2+) inhibition in ferritin C126S, was unpredicted. Identifying E57 and E136 links in Fe(2+) movement from ferritin ion channels to ferritin enzyme sites completes a bucket brigade that moves external Fe(2+) into ferritin enzymatic sites. The results clarify Fe(2+) transport within ferritin and model molecular links between membrane ion channels and cytoplasmic destinations.

Topics: Animals; Antioxidants; Anura; Catalysis; Conserved Sequence; Ferric Compounds; Ferritins; Heme; Hydroxides; Ion Channels; Iron; Metals; Minerals; Models, Chemical; Mutagenesis, Site-Directed; Oxidoreductases; Protein Structure, Secondary; Protein Structure, Tertiary; Substrate Specificity; Sulfates

Reduction of hexavalent Cr(VI) to the trivalent state is the common strategy for remediation of Cr(VI) contaminated waters and soils. In the presence of Fe the resulting compounds are usually mixed Fe(III)-Cr(III) phases, while, under iron-free conditions, reduction leads to formation of plain Cr(III) hydroxides. Environmental stability of these compounds depends on their structure and is important to understand how different precipitation conditions affect the local atomic order of resulting compounds and thus their long term stability. In current study, typical Cr(VI) environmental remediation products, i.e. plain and mixed Fe(III)-Cr(III) hydroxides, were synthesized by hydrolysis and redox reactions and their structure was studied by X ray diffraction and X ray absorption fine structure techniques. Plain Cr(III) hydroxide was found to correspond to the molecular formula Cr(OH)3·3H2O and was identified as crystalline in XRD. However, the same compound when examined by EXAFS did not exhibit any clear local order in the range of EXAFS detectable distances, i.e. between 0 and 5Å. Namely, EXAFS spectroscopy detected only contribution from the first nearest neighboring (Cr-O) shell, suggesting that CrO6 octahedra interconnection is loose, in accordance with the suggested anti-bayerite structure of this compound. Mixed Fe(III)-Cr(III) systems resembled 2-line ferrihydrite irrespective of the synthesis route. Analysis of Fe-K-EXAFS and Cr-K-EXAFS spectra indicated that FeO6 octahedra are bonded by sharing both edges and corners, while CrO6 octahedra seem to prefer edge sharing linkage. EXAFS data also suggest that Fe-Cr hydroxide produced by hydrolysis presents a better arrangement of CrO6 octahedra compared to the redox product.

Topics: Chromium; Environmental Restoration and Remediation; Ferric Compounds; Hydroxides; Oxidation-Reduction; X-Ray Absorption Spectroscopy; X-Ray Diffraction