In all cases, immediate medical attention should be obtained (fisher scientific, 2009). If it does not breathe, artificial respiration should be given. In case of inhalation, remove the victim from the exposure area and move to a cool place. Never give anything by mouth to an unconscious person. If swallowed, if the victim is conscious and alert, he should be given 2-4 cups of milk or water. If the compound comes into contact with the skin, it should be rinsed with copious amounts of water for at least 15 minutes while removing contaminated clothing and shoes. In case of contact with eyes, they should be rinsed with plenty of water for at least 15 minutes, occasionally lifting the upper and lower eyelids. The compound is very dangerous in case of ingestion and dangerous in case of contact with the eyes (irritant) and inhalation (Material Safety Data Sheet Ferrous sulfide, 2013). Reacts with oxidizing agents and when heated decomposes emits toxic fumes of sulfur oxides. The compound is pyrophoric and may ignite spontaneously or also the product of a strong impact, so it is not advisable to grind it in a mortar when it is synthesized and must be treated with care. Reacts with dilute solutions of sulfuric acid to form ferrous oxide, sulfur dioxide and water according to the reaction:įeS + H 2 SW 4 → FeO + H 2 O + SO 2 Reactivity and hazardsįerrous sulfide is an unstable compound and reacts with air to form ferrous oxide and sulfur. This is observed in the following reaction: It has a melting point of 1195 ° C and is insoluble in water and nitric acid (Royal Society of Chemistry, 2015).įerrous sulfide reacts in acid media to form ferrous oxide and hydrogen sulphide vapors that are extremely toxic. The compound has a molecular weight of 87.910 g / mol and a density of 4.84 g / ml. Figure 2 shows the appearance of ferrous sulfide. When it is pure it is colorless (National Center for Biotechnology Information, S.F.). Iron (II) sulfide is a dark brown or black metal-looking solid. Physical and chemical properties of iron sulfide (II) Subsequently iron (II) sulfate decomposes to ferrous sulfate, although the reaction occurs very slowly (Rickard, 1995). However, this reaction competes with the iron (II) sulfate formation reaction as follows: The sulfur, upon dissolving, forms hydrogen sulfide which reacts reversibly with the iron (II) ions according to the reaction S2CID 22085836.The reaction is very exothermic (releases heat) and the ratio of iron to sulfur should be 7: 4 (NileRed, 2014).įigure 1: Structure of iron (II) sulphide.įerrous sulfide may also be obtained in aqueous medium by dissolving sulfur in an ionic solution of iron (II). "MutY catalytic core, mutant and bound adenine structures define specificity for DNA repair enzyme superfamily". ^ BIOLOGICAL INORGANIC CHEMISTRY : structure and reactivity."Synthetic Analogues of the Active Sites of Iron-Sulfur Proteins". : CS1 maint: uses authors parameter ( link) Substitution of Sulfur by Selenium in the Series 2- X = S/Se and Y = S/Se". "Application of a Universal Force Field to Mixed Fe/Mo−S/Se Cubane and Heterocubane Clusters. ^ Axel Kern, Christian Näther, Felix Studt, Felix Tuczek (2004).Examples include endonuclease III and MutY. In some instances Fe–S clusters are redox-inactive, but are proposed to have structural roles. Both are part of the electron transport chain of their respective organisms which is a crucial step in the energy harvesting for many organisms. These photosynthetic organisms include plants, green algae, and cyanobacteria, the bacterial precursor to chloroplasts. They are also a part of the proteins of the chloroplast such as the cytochrome b 6f complex in photosynthetic organisms. The Rieske proteins contain Fe–S clusters that coordinate as a 2Fe–2S structure and can be found in the membrane bound cytochrome bc1 complex III in the mitochondria of eukaryotes and bacteria. Variations have been prepared including the incomplete cubanes 3−. Many clusters have been synthesized in the laboratory with the formula 2−, which are known for many R substituents, and with many cations. The relevant redox couple in all Fe–S proteins is Fe(II)/Fe(III). Both adopt cuboidal structures, but they utilize different oxidation states. The clusters occur in two forms: normal ferredoxins and high potential iron proteins (HiPIP). įe–S clusters can be classified according to their Fe:S stoichiometry, ,, and. They feature either 2Fe–2S or 4Fe–4S centers. The ferredoxin proteins are the most common Fe–S clusters in nature. Iron–sulfur clusters occur in many biological systems, often as components of electron transfer proteins.
0 Comments
Leave a Reply. |
AuthorWrite something about yourself. No need to be fancy, just an overview. ArchivesCategories |