Ricerc@Sapienza

The discovery of the ferroportin-hepcidin complex has led to a critical review on the treatment of anemia and anemia of inflammation (AI). Ferroportin, the only known mammalian iron exporter from cells to blood, is negatively regulated by hepcidin, a hormone peptide able to bind to ferroportin, leading to its degradation. Therefore, new efficient therapeutic interventions acting on hepcidin and ferroportin are imperative to manage anemia and AI.

Iron and its role as soul of life on Earth is addressed in this review as iron is one of the most abundant elements of our universe, forms the core of our planet and that of telluric (i.e., Earth-like) planets, is a major element of the Earth's crust and is hosted in an endless number of mineral phases, both crystalline and amorphous. To study iron at an atomic level inside the bulk of mineral phases or at its surface, where it is more reactive, both spectroscopy and diffraction experimental methods can be used, taking advantage of nearly the whole spectrum of electromagnetic waves.

Fep1, the iron-dependent GATA-type transcriptional repressor of the methylotrophic yeast Pichia pastoris, has a dimeric structure and binds an iron–sulfur cluster of the [2Fe–2S] type. In this work, we extend the characterization of this protein by analysis of the optical and CD spectroscopic properties of a set of mutants where cysteines within the conserved Cys-X5-Cys-X8-Cys-X2-Cys motif have been targeted, in order to evaluate their role as [2Fe–2S] ligands.

In the last 20 years, several new genes and proteins involved in iron metabolism in eukaryotes, particularly related to pathological states both in animal models and in humans have been identified, and we are now starting to unveil at the molecular level the mechanisms of iron absorption, the regulation of iron transport and the homeostatic balancing processes. In this review, we will briefly outline the general scheme of iron metabolism in humans and then focus our attention on the cellular iron export system formed by the permease ferroportin and the ferroxidase ceruloplasmin.

Down Syndrome (DS) is the most common genetic form of intellectual disability that leads in the majority of cases to development of early-onset Alzheimer-like dementia (AD). The neuropathology of DS has several common features with AD including alteration of redox homeostasis, mitochondrial deficits, and inflammation among others. Interestingly, some of the genes encoded by chromosome 21 are responsible of increased oxidative stress (OS) conditions that are further exacerbated by decreased antioxidant defense.

Ferroptosis is an iron-dependent form of regulated cell death, arising from the accumulation of lipid-based reactive oxygen species when glutathione-dependent repair systems are compromised. Lipid peroxidation, mitochondrial impairment and iron dyshomeostasis are the hallmark of ferroptosis, which is emerging as a crucial player in neurodegeneration.

The aim of the present experimental study was to perform a technical-economic evaluation of a combined treatment system, consisting of coagulation-flocculation or rapid sand filtration as pre-treatment followed by column adsorption, for reducing the arsenic concentration from approximately 1 mg/L to below the limit set for groundwater remediation and drinking water, i.e., 0.01 mg/L, according to the legislation in force. A wide number of operating conditions were experimentally evaluated in the different tests.

Time-resolved X-ray absorption (XAS) and UV-vis spectroscopies with millisecond resolution are used simultaneously to investigate oxidation reactions of organic substrates by nonheme iron activated species. In particular, the oxidation processes of arylsulfides and benzyl alcohols by a nonheme iron-oxo complex have been studied. We show for the first time that the pseudo-first-order rate constants of fast bimolecular processes in solution (milliseconds and above) can be determined by time-resolved XAS technique.

Substrate-selectivity stemming from recognition is a key feature of enzymes that has been seldom observed in artificial catalysts. Herein, we report a recognition-driven, substrate-selective C-H oxidation that inverts the intrinsic reactivity of the competing C-H bonds. Analysis of this selectivity highlights an unexpectedly high reactivity enhancement imparted by intramolecularity. © 2019 The Royal Society of Chemistry.

The civitas of Leopoli-Cencelle, founded by Pope Leo IV (9th cent.), is located in the Tolfa Mountains on the northern edge of the Province of Rome. The site has been the object of archaeological research directed by the Department of Medieval Archaeology at La Sapienza University of Rome. The paper focuses on the analysis of about thirty agricultural artefacts (hoes, sickles, billhooks and axes) originating from stratigraphic contexts corresponding to the town’s communal facies (13th-14th cent.).