Ferric Iron
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Ferric Iron
In chemistry, iron(III) refers to the element iron in its +3 oxidation state. In ionic compounds (salts), such an atom may occur as a separate cation (positive ion) denoted by Fe3+. The adjective ferric or the prefix ferri- is often used to specify such compounds — as in "ferric chloride" for iron(III) chloride, . The adjective "ferrous" is used instead for iron(II) salts, containing the cation Fe2+. The word ferric is derived from the Latin word ''ferrum'' for iron. Iron(III) metal centres also occur in coordination complexes, such as in the anion ferrioxalate, , where three bidentate oxalate ions surrounding the metal centre; or, in organometallic compounds, such as the ferrocenium cation , where two cyclopentadienyl anions are bound to the FeIII centre. Iron is almost always encountered in the oxidation states 0 (as in the metal), +2, or +3. Iron(III) is usually the most stable form in air, as illustrated by the pervasiveness of rust, an insoluble iron(III)-contain ...
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Iron(III)-oxide-sample
Iron () is a chemical element with symbol Fe (from la, ferrum) and atomic number 26. It is a metal that belongs to the first transition series and group 8 of the periodic table. It is, by mass, the most common element on Earth, right in front of oxygen (32.1% and 30.1%, respectively), forming much of Earth's outer and inner core. It is the fourth most common element in the Earth's crust. In its metallic state, iron is rare in the Earth's crust, limited mainly to deposition by meteorites. Iron ores, by contrast, are among the most abundant in the Earth's crust, although extracting usable metal from them requires kilns or furnaces capable of reaching or higher, about higher than that required to smelt copper. Humans started to master that process in Eurasia during the 2nd millennium BCE and the use of iron tools and weapons began to displace copper alloys, in some regions, only around 1200 BCE. That event is considered the transition from the Bronze Age to the Iron Age. In ...
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Ferrocenium
Ferrocenium tetrafluoroborate is an organometallic compound with the formula e(C5H5)2F4. This salt is composed of the cation e(C5H5)2sup>+ and the tetrafluoroborate anion (). The related hexafluorophosphate is also a popular reagent with similar properties. The cation is often abbreviated Fc+ or Cp2Fe+. The salt is deep blue in color and paramagnetic. Ferrocenium salts are sometimes used as one-electron oxidizing agents, and the reduced product, ferrocene, is inert and readily separated from ionic products. The ferrocene–ferrocenium couple is often used as a reference in electrochemistry. The standard potential of ferrocene-ferrocenium is 0.400 V vs. the normal hydrogen electrode (NHE) and is often assumed to be invariant between different solvents. Preparation Commercially available, this compound may be prepared by oxidizing ferrocene typically with ferric salts followed by addition of fluoroboric acid. A variety of other oxidants work well also, such as nitrosyl tet ...
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Calcareous Soil
Calcareous () is an adjective meaning "mostly or partly composed of calcium carbonate", in other words, containing lime or being chalky. The term is used in a wide variety of scientific disciplines. In zoology ''Calcareous'' is used as an adjectival term applied to anatomical structures which are made primarily of calcium carbonate, in animals such as gastropods, i.e., snails, specifically about such structures as the operculum, the clausilium, and the love dart. The term also applies to the calcium carbonate tests of often more or less microscopic Foraminifera. Not all tests are calcareous; diatoms and radiolaria have siliceous tests. The molluscs are calcareous, as are calcareous sponges (Porifera), that have spicules which are made of calcium carbonate. In botany ''Calcareous grassland'' is a form of grassland characteristic of soils containing much calcium carbonate from underlying chalk or limestone rock. In medicine The term is used in pathology, for example in ...
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Oxygen
Oxygen is the chemical element with the symbol O and atomic number 8. It is a member of the chalcogen group in the periodic table, a highly reactive nonmetal, and an oxidizing agent that readily forms oxides with most elements as well as with other compounds. Oxygen is Earth's most abundant element, and after hydrogen and helium, it is the third-most abundant element in the universe. At standard temperature and pressure, two atoms of the element bind to form dioxygen, a colorless and odorless diatomic gas with the formula . Diatomic oxygen gas currently constitutes 20.95% of the Earth's atmosphere, though this has changed considerably over long periods of time. Oxygen makes up almost half of the Earth's crust in the form of oxides.Atkins, P.; Jones, L.; Laverman, L. (2016).''Chemical Principles'', 7th edition. Freeman. Many major classes of organic molecules in living organisms contain oxygen atoms, such as proteins, nucleic acids, carbohydrates, and ...
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Anemia
Anemia or anaemia (British English) is a blood disorder in which the blood has a reduced ability to carry oxygen due to a lower than normal number of red blood cells, or a reduction in the amount of hemoglobin. When anemia comes on slowly, the symptoms are often vague, such as tiredness, weakness, shortness of breath, headaches, and a reduced ability to exercise. When anemia is acute, symptoms may include confusion, feeling like one is going to pass out, loss of consciousness, and increased thirst. Anemia must be significant before a person becomes noticeably pale. Symptoms of anemia depend on how quickly hemoglobin decreases. Additional symptoms may occur depending on the underlying cause. Preoperative anemia can increase the risk of needing a blood transfusion following surgery. Anemia can be temporary or long term and can range from mild to severe. Anemia can be caused by blood loss, decreased red blood cell production, and increased red blood cell breakdown. Causes ...
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Ferritin
Ferritin is a universal intracellular protein that stores iron and releases it in a controlled fashion. The protein is produced by almost all living organisms, including archaea, bacteria, algae, higher plants, and animals. It is the primary ''intracellular iron-storage protein'' in both prokaryotes and eukaryotes, keeping iron in a soluble and non-toxic form. In humans, it acts as a buffer against iron deficiency and iron overload. Ferritin is found in most tissues as a cytosolic protein, but small amounts are secreted into the serum (blood), serum where it functions as an iron carrier. Plasma ferritin is also an indirect biomarker, marker of the total amount of iron stored in the body; hence, serum ferritin is used as a diagnostic test for iron-deficiency anemia. Aggregated ferritin transforms into a toxic form of iron called hemosiderin. Ferritin is a globular protein complex consisting of 24 protein subunits forming a hollow nanocage with multiple metal–protein interacti ...
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Iron(III) Oxide Hydroxide
Iron(III) oxide-hydroxide or ferric oxyhydroxideA. L. Mackay (1960): "β-Ferric Oxyhydroxide". ''Mineralogical Magazine'' (''Journal of the Mineralogical Society''), volume 32, issue 250, pages 545-557. is the chemical compound of iron, oxygen, and hydrogen with formula . The compound is often encountered as one of its hydrates, ·''n'' ust The monohydrate · is often referred to as iron(III) hydroxide ,CAS , C.I. 77492 hydrated iron oxide, yellow iron oxide, or Pigment Yellow 42. Natural occurrences Minerals Anhydrous ferric hydroxide occurs in the nature as the exceedingly rare mineral bernalite, Fe(OH)3·''n''H2O (n=0.0-0.25). Iron oxyhydroxides, , are much more common and occur naturally as structurally different minerals (polymorphs) denoted by the Greek letters α, β, γ and δ. * Goethite, α-FeO(OH), has been used as an ochre pigment since prehistoric times. * Akaganeite is the β polymorph,A. L. Mackay (1962): "β-Ferric oxyhydroxide—akaganéite", ''Minera ...
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Cytochrome
Cytochromes are redox-active proteins containing a heme, with a central Fe atom at its core, as a cofactor. They are involved in electron transport chain and redox catalysis. They are classified according to the type of heme and its mode of binding. Four varieties are recognized by the International Union of Biochemistry and Molecular Biology (IUBMB), cytochromes a, cytochromes b, cytochromes c and cytochrome d. Cytochrome function is linked to the reversible redox change from ferrous (Fe(II)) to the ferric (Fe(III)) oxidation state of the iron found in the heme core. In addition to the classification by the IUBMB into four cytochrome classes, several additional classifications such as cytochrome o and cytochrome P450 can be found in biochemical literature. History Cytochromes were initially described in 1884 by Charles Alexander MacMunn as respiratory pigments (myohematin or histohematin). In the 1920s, Keilin rediscovered these respiratory pigments and named them the ...
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Ferredoxin
Ferredoxins (from Latin ''ferrum'': iron + redox, often abbreviated "fd") are iron–sulfur proteins that mediate electron transfer in a range of metabolic reactions. The term "ferredoxin" was coined by D.C. Wharton of the DuPont Co. and applied to the "iron protein" first purified in 1962 by Mortenson, Valentine, and Carnahan from the anaerobic bacterium '' Clostridium pasteurianum''. Another redox protein, isolated from spinach chloroplasts, was termed "chloroplast ferredoxin". The chloroplast ferredoxin is involved in both cyclic and non-cyclic photophosphorylation reactions of photosynthesis. In non-cyclic photophosphorylation, ferredoxin is the last electron acceptor thus reducing the enzyme NADP+ reductase. It accepts electrons produced from sunlight- excited chlorophyll and transfers them to the enzyme ferredoxin: NADP+ oxidoreductase . Ferredoxins are small proteins containing iron and sulfur atoms organized as iron–sulfur clusters. These biological "capacitors" can ...
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Oxyhemoglobin
Hemoglobin (haemoglobin BrE) (from the Greek word αἷμα, ''haîma'' 'blood' + Latin ''globus'' 'ball, sphere' + ''-in'') (), abbreviated Hb or Hgb, is the iron-containing oxygen-transport metalloprotein present in red blood cells (erythrocytes) of almost all vertebrates (the exception being the fish family Channichthyidae) as well as the tissues of some invertebrates. Hemoglobin in blood carries oxygen from the respiratory organs (''e.g.'' lungs or gills) to the rest of the body (''i.e.'' tissues). There it releases the oxygen to permit aerobic respiration to provide energy to power functions of an organism in the process called metabolism. A healthy individual human has 12to 20grams of hemoglobin in every 100mL of blood. In mammals, the chromoprotein makes up about 96% of the red blood cells' dry content (by weight), and around 35% of the total content (including water). Hemoglobin has an oxygen-binding capacity of 1.34mL O2 per gram, which increases the total blood oxygen ca ...
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Metalloprotein
Metalloprotein is a generic term for a protein that contains a metal ion cofactor. A large proportion of all proteins are part of this category. For instance, at least 1000 human proteins (out of ~20,000) contain zinc-binding protein domains although there may be up to 3000 human zinc metalloproteins. Abundance It is estimated that approximately half of all proteins contain a metal. In another estimate, about one quarter to one third of all proteins are proposed to require metals to carry out their functions. Thus, metalloproteins have many different functions in cells, such as storage and transport of proteins, enzymes and signal transduction proteins, or infectious diseases. The abundance of metal binding proteins may be inherent to the amino acids that proteins use, as even artificial proteins without evolutionary history will readily bind metals. Most metals in the human body are bound to proteins. For instance, the relatively high concentration of iron in the human body is ...
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Protein
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called peptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid ...
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