How to name new chemical elements (IUPAC Recommendations 2016)

A procedure is proposed to name new chemical elements. After the discovery of a new element is established by the joint IUPAC-IUPAP Working Group, the discoverers are invited to propose a name and a symbol to the IUPAC Inorganic Chemistry Division. Elements can be named after a mythological concept, a mineral, a place or country, a property or a scientist. After examination and acceptance by the Inorganic Chemistry Division, the proposal follows the accepted IUPAC procedure and is then ratified by the Council of IUPAC. This document is a slightly amended version of the 2002 IUPAC Recommendations; the most important change is that the names of all new elements should have an ending that reflects and maintains historical and chemical consistency. This would be in general "-ium" for elements belonging to groups 1-16, i.e. including the f-block elements, "-ine" for elements of group 17 and "-on" for elements of group 18.Metals in Catalysis, Biomimetics & Inorganic Material

Iron and Its Catalytic Properties on Radical Generation: Role of chelators on the labile iron pool (LIP)

Iron (Fe) is an essential element for the growth and well-being of almost all living organisms as it is involved in many biological functions since by varying the ligands to which it is coordinated. Fe has access to a wide range of redox potentials and can participate in many electron transfer reactions, spanning the standard redox potential range. It is also involved in O2 transport, activation, and detoxification, in N2 fixation and in several of the reactions of photosynthesis. However, there are problems in the physiological management of Fe. Anytime Fe exceeds the metabolic needs of the cell it may form low molecular weight pool, referred as the labile iron pool (LIP), which catalyzed the conversion of normal by-products of cell respiration, like superoxide anion (O2-) and hydrogen peroxide (H2O2), into highly damaging hydroxyl radical (?OH) through the Fenton reaction or by the Fe2+-catalyzed Haber-Weiss reaction, or into equally aggressive ferryl ions or O2-bridged Fe2+/Fe3+ complexes. Fe3+ can be reduced either by O2- or by ascorbate (AH-) leading to further radical production. The LIP consists of Fe2+ and Fe3+ associated with a variety of ligands with low affinity for Fe ions. However, the intracellular ligands participating in LIP formation remains obscure and the accessibility of cellular Fe to chelators is commonly used as the criterion of ´lability´. This chapter was intended to summarize the current knowledge on the nature and the function of LIP in cellular oxidative conditions.Fil: Robello, Elizabeth. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Bioquímica y Medicina Molecular. Universidad de Buenos Aires. Facultad Medicina. Instituto de Bioquímica y Medicina Molecular; ArgentinaFil: Galatro, Andrea Verónica. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Fisiología Vegetal. Universidad Nacional de La Plata. Facultad de Ciencias Naturales y Museo. Instituto de Fisiología Vegetal; ArgentinaFil: Puntarulo, Susana Ángela. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Bioquímica y Medicina Molecular. Universidad de Buenos Aires. Facultad Medicina. Instituto de Bioquímica y Medicina Molecular; Argentin

Electron-transfer‐mediated binding of optically active cobalt(III) complexes to horse heart cytochrome c

Optically active cobalt(II) complexes are used as reducing agents in the electron-transfer reaction involving horse heart cytochrome c. Analysis of the circular dichroism (CD) spectra of reaction products indicates that the corresponding cobalt(III) species of both enantiomers of [Co(II)(alamp)] (H(2)alamp=N,N′-[(pyridine-2,6-diyl)bis(methylene)]-bis[alanine]) are partly attached to the protein during electron transfer by coordination to an imidazole unit of one of the histidine residues. His-26 and His-33 are both solvent exposed, and the results suggest that one of these histidine residues acts as a bridge in the electron transfer to and from the haem iron of cytochrome c. The reaction is enantioselective: the ratio of the relative reactivity at 15 °C is 2.9 in favour of the R,R-enantiomer. A small induced CD activity in the haem chromophore reveals that some structural changes in the protein occur consecutively with the binding of the cobalt(III) complex