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Methane Monooxygenase
Methane monooxygenase (MMO) is an enzyme capable of oxidizing the C-H bond in methane as well as other alkanes. Methane monooxygenase belongs to the class of oxidoreductase enzymes (). There are two forms of MMO: the well-studied soluble form (sMMO) and the particulate form (pMMO). The active site in sMMO contains a di-iron center bridged by an oxygen atom (Fe-O-Fe), whereas the active site in pMMO utilizes copper. Structures of both proteins have been determined by X-ray crystallography; however, the location and mechanism of the active site in pMMO is still poorly understood and is an area of active research. The particulate methane monooxygenase and related ammonia monooxygenase are integral membrane proteins, occurring in methanotrophs and ammonia oxidisers, respectively, which are thought to be related. These enzymes have a relatively wide substrate specificity and can catalyse the oxidation of a range of substrates including ammonia, methane, halogenated hydrocarbons, and ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Methane
Methane ( , ) is a chemical compound with the chemical formula (one carbon atom bonded to four hydrogen atoms). It is a group-14 hydride, the simplest alkane, and the main constituent of natural gas. The relative abundance of methane on Earth makes it an economically attractive fuel, although capturing and storing it poses technical challenges due to its gaseous state under normal conditions for temperature and pressure. Naturally occurring methane is found both below ground and under the seafloor and is formed by both geological and biological processes. The largest reservoir of methane is under the seafloor in the form of methane clathrates. When methane reaches the surface and the atmosphere, it is known as atmospheric methane. The Earth's atmospheric methane concentration has increased by about 150% since 1750, and it accounts for 20% of the total radiative forcing from all of the long-lived and globally mixed greenhouse gases. It has also been detected on other plane ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ferromagnetic
Ferromagnetism is a property of certain materials (such as iron) which results in a large observed magnetic permeability, and in many cases a large magnetic coercivity allowing the material to form a permanent magnet. Ferromagnetic materials are the familiar metals noticeably attracted to a magnet, a consequence of their large magnetic permeability. Magnetic permeability describes the induced magnetization of a material due to the presence of an ''external'' magnetic field, and it is this temporarily induced magnetization inside a steel plate, for instance, which accounts for its attraction to the permanent magnet. Whether or not that steel plate acquires a permanent magnetization itself, depends not only on the strength of the applied field, but on the so-called coercivity of that material, which varies greatly among ferromagnetic materials. In physics, several different types of material magnetism are distinguished. Ferromagnetism (along with the similar effect ferrimagneti ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Oxidoreductases
In biochemistry, an oxidoreductase is an enzyme that catalyzes the transfer of electrons from one molecule, the reductant, also called the electron donor, to another, the oxidant, also called the electron acceptor. This group of enzymes usually utilizes NADP+ or NAD+ as cofactors. Transmembrane oxidoreductases create electron transport chains in bacteria, chloroplasts and mitochondria, including respiratory complexes I, II and III. Some others can associate with biological membranes as peripheral membrane proteins or be anchored to the membranes through a single transmembrane helix. in Re ...
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Metalloproteins
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 i ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Copper Enzymes
Copper is a chemical element with the symbol Cu (from la, cuprum) and atomic number 29. It is a soft, malleable, and ductile metal with very high thermal and electrical conductivity. A freshly exposed surface of pure copper has a pinkish-orange color. Copper is used as a conductor of heat and electricity, as a building material, and as a constituent of various metal alloys, such as sterling silver used in jewelry, cupronickel used to make marine hardware and coins, and constantan used in strain gauges and thermocouples for temperature measurement. Copper is one of the few metals that can occur in nature in a directly usable metallic form (native metals). This led to very early human use in several regions, from circa 8000 BC. Thousands of years later, it was the first metal to be smelted from sulfide ores, circa 5000 BC; the first metal to be cast into a shape in a mold, c. 4000 BC; and the first metal to be purposely alloyed with another metal, tin, to create bronze, c. ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Enzymes
Enzymes () are proteins that act as biological catalysts by accelerating chemical reactions. The molecules upon which enzymes may act are called substrate (chemistry), substrates, and the enzyme converts the substrates into different molecules known as product (chemistry), products. Almost all metabolism, metabolic processes in the cell (biology), cell need enzyme catalysis in order to occur at rates fast enough to sustain life. Metabolic pathways depend upon enzymes to catalyze individual steps. The study of enzymes is called ''enzymology'' and the field of pseudoenzyme, pseudoenzyme analysis recognizes that during evolution, some enzymes have lost the ability to carry out biological catalysis, which is often reflected in their amino acid sequences and unusual 'pseudocatalytic' properties. Enzymes are known to catalyze more than 5,000 biochemical reaction types. Other biocatalysts are Ribozyme, catalytic RNA molecules, called ribozymes. Enzymes' Chemical specificity, specific ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Shilov System
The Shilov system is a classic example of catalytic C-H bond activation and oxidation which preferentially activates stronger C-H bonds over weaker C-H bonds for an overall partial oxidation. C. I. Herrerias, X. Yao, Z. Li, C.-J. Li, Reactions of C-H Bonds in Water, ''Chem. Rev.''; 2007; 107(6); 2546-2562. Overview The Shilov system was discovered by Alexander E. Shilov in 1969-1972 while investigating H/D exchange between isotopologues of CH4 and H2O catalyzed simple transition metal coordination complexes. The Shilov cycle is the partial oxidation of a hydrocarbon to an alcohol or alcohol precursor (RCl) catalyzed by PtIICl2 in an aqueous solution with 2−.html" ;"title="tIVCl6sup>2−">tIVCl6sup>2− acting as the ultimate oxidant. The cycle consists of three major steps, the electrophilic activation of the C-H bond, oxidation of the complex, and the nucleophilic oxidation of the alkane substrate. An equivalent transformation is performed industrially by steam refor ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Oxygenase
An oxygenase is any enzyme that oxidizes a substrate by transferring the oxygen from molecular oxygen O2 (as in air) to it. The oxygenases form a class of oxidoreductases; their EC number is EC 1.13 or EC 1.14. Discoverers Oxygenases were discovered in 1955 simultaneously by two groups, Osamu Hayaishi from Japan and Howard S. Mason from the US. Hayaishi was awarded the 1986 Wolf Prize in Medicine "for the discovery of the oxygenase enzymes and elucidation of their structure and biological importance." Chemical Makeup Oxygenases consist of both constitutive and inducible isozymes (HO-1, HO-2). These constitute a major intracellular source of iron and carbon monoxide Types There are two types of oxygenases: *Monooxygenases, or mixed function oxidase, transfer one oxygen atom to the substrate, and reduce the other oxygen atom to water. *Dioxygenases, or oxygen transferases, incorporate both atoms of molecular oxygen (O2) into the product(s) of the reaction. Among the most impor ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Bioinorganic Chemistry
Bioinorganic chemistry is a field that examines the role of metals in biology. Bioinorganic chemistry includes the study of both natural phenomena such as the behavior of metalloproteins as well as artificially introduced metals, including those that are non-essential, in medicine and toxicology. Many biological processes such as respiration depend upon molecules that fall within the realm of inorganic chemistry. The discipline also includes the study of inorganic models or mimics that imitate the behaviour of metalloproteins. As a mix of biochemistry and inorganic chemistry, bioinorganic chemistry is important in elucidating the implications of electron-transfer proteins, substrate bindings and activation, atom and group transfer chemistry as well as metal properties in biological chemistry. The successful development of truly interdisciplinary work is necessary to advance bioinorganic chemistry. Composition of living organisms About 99% of mammals' mass are the elements carb ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Antiferromagnetism
In materials that exhibit antiferromagnetism, the magnetic moments of atoms or molecules, usually related to the spins of electrons, align in a regular pattern with neighboring spins (on different sublattices) pointing in opposite directions. This is, like ferromagnetism and ferrimagnetism, a manifestation of ordered magnetism. The phenomenon of antiferromagnetism was first introduced by Lev Landau in 1933. Generally, antiferromagnetic order may exist at sufficiently low temperatures, but vanishes at and above the Néel temperature – named after Louis Néel, who had first identified this type of magnetic ordering. Above the Néel temperature, the material is typically paramagnetic. Measurement When no external field is applied, the antiferromagnetic structure corresponds to a vanishing total magnetization. In an external magnetic field, a kind of ferrimagnetic behavior may be displayed in the antiferromagnetic phase, with the absolute value of one of the sublattice magneti ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
