FerredoxinFerredoxins (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".
Iron-sulfur proteinIron–sulfur proteins are proteins characterized by the presence of iron–sulfur clusters containing sulfide-linked di-, tri-, and tetrairon centers in variable oxidation states. Iron–sulfur clusters are found in a variety of metalloproteins, such as the ferredoxins, as well as NADH dehydrogenase, hydrogenases, coenzyme Q – cytochrome c reductase, succinate – coenzyme Q reductase and nitrogenase. Iron–sulfur clusters are best known for their role in the oxidation-reduction reactions of electron transport in mitochondria and chloroplasts.
MetalloproteinMetalloprotein 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. 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.
HydrogenaseA hydrogenase is an enzyme that catalyses the reversible oxidation of molecular hydrogen (H2), as shown below: Hydrogen uptake () is coupled to the reduction of electron acceptors such as oxygen, nitrate, sulfate, carbon dioxide (), and fumarate. On the other hand, proton reduction () is coupled to the oxidation of electron donors such as ferredoxin (FNR), and serves to dispose excess electrons in cells (essential in pyruvate fermentation).
RubredoxinRubredoxins are a class of low-molecular-weight iron-containing proteins found in sulfur-metabolizing bacteria and archaea. Sometimes rubredoxins are classified as iron-sulfur proteins; however, in contrast to iron-sulfur proteins, rubredoxins do not contain inorganic sulfide. Like cytochromes, ferredoxins and Rieske proteins, rubredoxins are thought to participate in electron transfer in biological systems. Recent work in bacteria and algae have led to the hypothesis that some rubredoxins may instead have a role in delivering iron to metalloproteins.
Iron–sulfur clusterIron–sulfur clusters are molecular ensembles of iron and sulfide. They are most often discussed in the context of the biological role for iron–sulfur proteins, which are pervasive. Many Fe–S clusters are known in the area of organometallic chemistry and as precursors to synthetic analogues of the biological clusters (see Figure). It is believed that the last universal common ancestor had many iron-sulfur clusters. Organometallic Fe–S clusters include the sulfido carbonyls with the formula Fe2S2(CO)6, H2Fe3S(CO)9, and Fe3S2(CO)9.
SiderophoreSiderophores (Greek: "iron carrier") are small, high-affinity iron-chelating compounds that are secreted by microorganisms such as bacteria and fungi. They help the organism accumulate iron. Although a widening range of siderophore functions is now being appreciated, siderophores are among the strongest (highest affinity) Fe3+ binding agents known. Phytosiderophores are siderophores produced by plants. Despite being one of the most abundant elements in the Earth's crust, iron is not readily bioavailable.
Inorganic chemistryInorganic chemistry deals with synthesis and behavior of inorganic and organometallic compounds. This field covers chemical compounds that are not carbon-based, which are the subjects of organic chemistry. The distinction between the two disciplines is far from absolute, as there is much overlap in the subdiscipline of organometallic chemistry. It has applications in every aspect of the chemical industry, including catalysis, materials science, pigments, surfactants, coatings, medications, fuels, and agriculture.
Metal aquo complexIn chemistry, metal aquo complexes are coordination compounds containing metal ions with only water as a ligand. These complexes are the predominant species in aqueous solutions of many metal salts, such as metal nitrates, sulfates, and perchlorates. They have the general stoichiometry . Their behavior underpins many aspects of environmental, biological, and industrial chemistry. This article focuses on complexes where water is the only ligand ("homoleptic aquo complexes"), but of course many complexes are known to consist of a mix of aquo and other ligands.
CobaltCobalt is a chemical element with the symbol Co and atomic number 27. As with nickel, cobalt is found in the Earth's crust only in a chemically combined form, save for small deposits found in alloys of natural meteoric iron. The free element, produced by reductive smelting, is a hard, lustrous, silver metal. Cobalt-based blue pigments (cobalt blue) have been used since ancient times for jewelry and paints, and to impart a distinctive blue tint to glass, but the color was for a long time thought to be due to the known metal bismuth.
