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Hemoprotein
A hemeprotein (or haemprotein; also hemoprotein or haemoprotein), or heme protein, is a protein that contains a heme prosthetic group. They are a very large class of metalloproteins. The heme group confers functionality, which can include oxygen carrying, oxygen reduction, electron transfer, and other processes. Heme is bound to the protein either covalently or noncovalently or both. The heme consists of iron cation bound at the center of the conjugate base of the porphyrin, as well as other ligands attached to the "axial sites" of the iron. The porphyrin ring is a planar dianionic, tetradentate ligand. The iron is typically Fe2+ or Fe3+. One or two ligands are attached at the axial sites. The porphyrin ring has four nitrogen atoms that bind to the iron, leaving two other coordination positions of the iron available for bonding to the histidine of the protein and a divalent atom. Hemeproteins probably evolved to incorporate the iron atom contained within the protoporphyrin ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Heme
Heme (American English), or haem (Commonwealth English, both pronounced /Help:IPA/English, hi:m/ ), is a ring-shaped iron-containing molecule that commonly serves as a Ligand (biochemistry), ligand of various proteins, more notably as a Prosthetic group, component of hemoglobin, which is necessary to bind oxygen in the bloodstream. It is composed of four pyrrole rings with 2 Vinyl group, vinyl and 2 propionic acid side chains. Heme is biosynthesized in both the bone marrow and the liver. Heme plays a critical role in multiple different redox reactions in mammals, due to its ability to carry the oxygen molecule. Reactions include oxidative metabolism (cytochrome c oxidase, succinate dehydrogenase), xenobiotic detoxification via cytochrome P450 pathways (including Drug metabolism, metabolism of some drugs), gas sensing (Guanylate cyclase, guanyl cyclases, nitric oxide synthase), and microRNA processing (DGCR8). Heme is a coordination complex "consisting of an iron ion coordinated ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Porphyrin
Porphyrins ( ) are heterocyclic, macrocyclic, organic compounds, composed of four modified pyrrole subunits interconnected at their α carbon atoms via methine bridges (). In vertebrates, an essential member of the porphyrin group is heme, which is a component of hemoproteins, whose functions include carrying oxygen in the bloodstream. In plants, an essential porphyrin derivative is chlorophyll, which is involved in light harvesting and electron transfer in photosynthesis. The parent of porphyrins is porphine, a rare chemical compound of exclusively theoretical interest. Substituted porphines are called porphyrins. With a total of 26 π-electrons the porphyrin ring structure is a coordinated aromatic system. One result of the large conjugated system is that porphyrins absorb strongly in the visible region of the electromagnetic spectrum, i.e. they are deeply colored. The name "porphyrin" derives . Structure Porphyrin complexes consist of a square planar MN4 core. The p ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Neuroglobin
Neuroglobin is a member of the vertebrate globin family involved in cellular oxygen homeostasis and reactive oxygen/nitrogen scavenging. It is an intracellular hemoprotein expressed in the central and peripheral nervous system, cerebrospinal fluid, retina and endocrine tissues. Neuroglobin is a monomer that reversibly binds oxygen with an affinity higher than that of hemoglobin. It also increases oxygen availability to brain tissue and provides protection under hypoxic or ischemic conditions, potentially limiting brain damage. Neuroglobin were in the past found only in vertebrate neurons, but recently in 2013, were found in the neurons of unrelated protostomes, like photosynthetic acoel as well as radiata such as jellyfish. In addition to neurons, neuroglobin is present in astrocytes in certain pathologies of the rodent brain and in the physiological seal brain. This is thought to be due to convergent evolution. It is of ancient evolutionary origin, and is homologous to nerve glob ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Myoglobin
Myoglobin (symbol Mb or MB) is an iron- and oxygen-binding protein found in the cardiac and skeletal muscle, skeletal Muscle, muscle tissue of vertebrates in general and in almost all mammals. Myoglobin is distantly related to hemoglobin. Compared to hemoglobin, myoglobin has a higher affinity for oxygen and does not have cooperative binding with oxygen like hemoglobin does. Myoglobin consists of non-polar amino acids at the core of the globulin, where the heme group is non-covalently bounded with the surrounding polypeptide of myoglobin. In humans, myoglobin is found in the bloodstream only after Strain (injury), muscle injury. (Google books link is the 2008 edition) High concentrations of myoglobin in muscle cells allow organisms to hold their breath for a longer period of time. Diving mammals such as whales and seals have muscles with particularly high abundance of myoglobin. Myoglobin is found in Type I muscle, Type II A, and Type II B; although many older texts describe myo ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cytochrome B
Cytochrome b is a protein found in the membranes of aerobic cells. In eukaryotic mitochondria (inner membrane) and in aerobic prokaryotes, cytochrome b is a component of respiratory chain complex III () — also known as the bc1 complex or ubiquinol-cytochrome c reductase. In plant chloroplasts and cyanobacteria, there is a homologous protein, cytochrome b6, a component of the plastoquinone-plastocyanin reductase (), also known as the b6f complex. These complexes are involved in electron transport, the pumping of protons to create a proton-motive force ( PMF). This proton gradient is used for the generation of ATP. These complexes play a vital role in cells. Structure and function Cytochrome b/b6 is an integral membrane protein of approximately 400 amino acid residues that probably has 8 transmembrane segments. In plants and cyanobacteria, cytochrome b6 consists of two protein subunits encoded by the petB and petD genes. Cytochrome b/b6 non-covalently binds two heme ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cytochrome C Oxidase
The enzyme cytochrome c oxidase or Complex IV (was , now reclassified as a translocasEC 7.1.1.9 is a large transmembrane protein complex found in bacteria, archaea, and the mitochondria of eukaryotes. It is the last enzyme in the Cellular respiration, respiratory electron transport chain of cell (biology), cells located in the membrane. It receives an electron from each of four cytochrome c molecules and transfers them to one oxygen molecule and four protons, producing two molecules of water. In addition to binding the four protons from the inner aqueous phase, it transports another four protons across the membrane, increasing the transmembrane difference of proton electrochemical potential, which the ATP synthase then uses to synthesize Adenosine triphosphate, ATP. Structure The complex The complex is a large integral membrane protein composed of several Cofactor (biochemistry)#Metal ions, metal prosthetic sites and 13 protein subunits in mammals. In mammals, ten subunits a ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Electron Transport Chain
An electron transport chain (ETC) is a series of protein complexes and other molecules which transfer electrons from electron donors to electron acceptors via redox reactions (both reduction and oxidation occurring simultaneously) and couples this electron transfer with the transfer of protons (H+ ions) across a membrane. Many of the enzymes in the electron transport chain are embedded within the membrane. The flow of electrons through the electron transport chain is an exergonic process. The energy from the redox reactions creates an electrochemical proton gradient that drives the synthesis of adenosine triphosphate (ATP). In aerobic respiration, the flow of electrons terminates with molecular oxygen as the final electron acceptor. In anaerobic respiration, other electron acceptors are used, such as sulfate. In an electron transport chain, the redox reactions are driven by the difference in the Gibbs free energy of reactants and products. The free energy released when ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Electron Transfer
Electron transfer (ET) occurs when an electron relocates from an atom, ion, or molecule, to another such chemical entity. ET describes the mechanism by which electrons are transferred in redox reactions. Electrochemical processes are ET reactions. ET reactions are relevant to photosynthesis and respiration and commonly involve transition metal complexes. In organic chemistry ET is a step in some industrial polymerization reactions. It is foundational to photoredox catalysis. Classes of electron transfer Inner-sphere electron transfer In inner-sphere ET, two redox centers are covalently linked during the ET. This bridge can be permanent, in which case the electron transfer event is termed intramolecular electron transfer. More commonly, however, the covalent linkage is transitory, forming just prior to the ET and then disconnecting following the ET event. In such cases, the electron transfer is termed intermolecular electron transfer. A famous example of an inner sphere ET pr ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Peroxidase
Peroxidases or peroxide reductases ( EC numberbr>1.11.1.x are a large group of enzymes which play a role in various biological processes. They are named after the fact that they commonly break up peroxides, and should not be confused with other enzymes that ''produce'' peroxide, which are often oxidases. Functionality Peroxidases typically catalyze a reaction of the form: :ROOR' + \overset + 2H+ -> ce + R'OH Optimal substrates For many of these enzymes the optimal substrate is hydrogen peroxide, but others are more active with organic hydroperoxides such as lipid peroxides. Peroxidases can contain a heme cofactor in their active sites, or alternately redox-active cysteine or selenocysteine residues. The nature of the electron donor is very dependent on the structure of the enzyme. * For example, horseradish peroxidase can use a variety of organic compounds as electron donors and acceptors. Horseradish peroxidase has an accessible active site, and many compounds can re ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Catalase
Catalase is a common enzyme found in nearly all living organisms exposed to oxygen (such as bacteria, plants, and animals) which catalyzes the decomposition of hydrogen peroxide to water and oxygen. It is a very important enzyme in protecting the cell from oxidative damage by reactive oxygen species (ROS). Catalase has one of the highest turnover numbers of all enzymes; one catalase molecule can convert millions of hydrogen peroxide molecules to water and oxygen each second. Catalase is a tetramer of four polypeptide chains, each over 500 amino acids long. It contains four iron-containing heme groups that allow the enzyme to react with hydrogen peroxide. The optimum pH for human catalase is approximately 7, and has a fairly broad maximum: the rate of reaction does not change appreciably between pH 6.8 and 7.5. The pH optimum for other catalases varies between 4 and 11 depending on the species. The optimum temperature also varies by species. Structure Human catalase for ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ligninase
Lignin-modifying enzymes (LMEs) are various types of enzymes produced by fungi and bacteria that catalyze the breakdown of lignin, a biopolymer commonly found in the cell walls of plants. The terms ligninases and lignases are older names for the same class, but the name "lignin-modifying enzymes" is now preferred, given that these enzymes are not hydrolytic but rather oxidative (electron withdrawing) by their enzymatic mechanisms. LMEs include peroxidases, such as lignin peroxidase (), manganese peroxidase (), versatile peroxidase (), and many phenoloxidases of the laccase type. LMEs have been known to be produced by many species of white rot basidiomycetous fungi, including: ''Phanerochaete chrysosporium'', '' Ceriporiopsis subvermispora'', '' Trametes versicolor'', '' Phlebia radiata'', ''Pleurotus ostreatus'' and '' Pleurotus eryngii''. LMEs are produced not only by wood-white rotting fungi but also by litter-decomposing basidiomycetous fungi such as ''Agaricus bisporus'' ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
