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Proton Channel
A proton pump is an integral membrane protein pump that builds up a proton gradient across a biological membrane. Proton pumps catalyze the following reaction: : n one side of a biological membrane/sub> + energy n the other side of the membrane/sub> Mechanisms are based on energy-induced conformational changes of the protein structure or on the Q cycle. During evolution, proton pumps have arisen independently on multiple occasions. Thus, not only throughout nature but also within single cells, different proton pumps that are evolutionarily unrelated can be found. Proton pumps are divided into different major classes of pumps that use different sources of energy, have different polypeptide compositions and evolutionary origins. Function Transport of the positively charged proton is typically electrogenic, i.e. it generates an electric field across the membrane also called the membrane potential. Proton transport becomes electrogenic if not neutralized electrically by tran ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Proton Beam
A charged particle beam is a spatially localized group of electrically charged particles that have approximately the same position, kinetic energy (resulting in the same velocity), and direction. The kinetic energies of the particles are much larger than the energies of particles at ambient temperature. The high energy and directionality of charged particle beams make them useful for many applications in particle physics (see Particle beam#Applications and Electron-beam technology). Such beams can be split into two main classes: # ''unbunched beams'' (''coasting beams'' or ''DC beams''), which have no longitudinal substructure in the direction of beam motion. # ''bunched beams'', in which the particles are distributed into pulses (bunches) of particles. Bunched beams are most common in modern facilities, since the most modern particle accelerators require bunched beams for acceleration. Assuming a normal distribution of particle positions and impulses, a charged particle ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Bacteriorhodopsin
Bacteriorhodopsin is a protein used by Archaea, most notably by haloarchaea, a class of the Euryarchaeota. It acts as a proton pump; that is, it captures light energy and uses it to move protons across the membrane out of the cell. The resulting proton gradient is subsequently converted into chemical energy. Function Bacteriorhodopsin is a light-driven H+ ion transporter found in some haloarchaea, most notably ''Halobacterium salinarum'' (formerly known as syn. ''H. halobium''). The proton-motive force generated by the protein is used by ATP synthase to generate adenosine triphosphate (ATP). By expressing bacteriorhodopsin, the archaea cells are able to synthesise ATP in the absence of a carbon source. Structure Bacteriorhodopsin is a 27 kDa integral membrane protein usually found in two-dimensional crystalline patches known as "purple membrane", which can occupy almost 50% of the surface area of the archaeal cell. The repeating element of the hexagonal lattice is compose ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Eukaryote
Eukaryotes () are organisms whose cells have a nucleus. All animals, plants, fungi, and many unicellular organisms, are Eukaryotes. They belong to the group of organisms Eukaryota or Eukarya, which is one of the three domains of life. Bacteria and Archaea (both prokaryotes) make up the other two domains. The eukaryotes are usually now regarded as having emerged in the Archaea or as a sister of the Asgard archaea. This implies that there are only two domains of life, Bacteria and Archaea, with eukaryotes incorporated among archaea. Eukaryotes represent a small minority of the number of organisms, but, due to their generally much larger size, their collective global biomass is estimated to be about equal to that of prokaryotes. Eukaryotes emerged approximately 2.3–1.8 billion years ago, during the Proterozoic eon, likely as flagellated phagotrophs. Their name comes from the Greek εὖ (''eu'', "well" or "good") and κάρυον (''karyon'', "nut" or "kernel"). E ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Coenzyme Q10
Coenzyme Q, also known as ubiquinone and marketed as CoQ10, is a coenzyme family that is ubiquitous in animals and most bacteria (hence the name ubiquinone). In humans, the most common form is coenzyme Q10 or ubiquinone-10. It is a 1,4-benzoquinone, where Q refers to the quinone chemical group and 10 refers to the number of isoprene, isoprenyl chemical subunits in its tail. In natural ubiquinones, the number can be anywhere from 6 to 10. This family of fat-soluble substances, which resemble vitamins, is present in all respiring eukaryotic cells, primarily in the mitochondria. It is a component of the electron transport chain and participates in aerobic cellular respiration, which generates energy in the form of ATP. Ninety-five percent of the human body's energy is generated this way. Organs with the highest energy requirements—such as the heart, liver, and kidney—have the highest CoQ10 concentrations. There are three redox states of CoQ: fully oxidized (ubiquinone), s ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Catalyze
Catalysis () is the process of increasing the rate of a chemical reaction by adding a substance known as a catalyst (). Catalysts are not consumed in the reaction and remain unchanged after it. If the reaction is rapid and the catalyst recycles quickly, very small amounts of catalyst often suffice; mixing, surface area, and temperature are important factors in reaction rate. Catalysts generally react with one or more reactants to form intermediates that subsequently give the final reaction product, in the process of regenerating the catalyst. Catalysis may be classified as either homogeneous, whose components are dispersed in the same phase (usually gaseous or liquid) as the reactant, or heterogeneous, whose components are not in the same phase. Enzymes and other biocatalysts are often considered as a third category. Catalysis is ubiquitous in chemical industry of all kinds. Estimates are that 90% of all commercially produced chemical products involve catalysts at some stag ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Mrp Superfamily
The Na+ Transporting Mrp Superfamily is a superfamily of integral membrane transport proteins. It includes the TC families:2.A.63- The Monovalent Cation (K+ or Na+):Proton Antiporter-3 (CPA3) Family3.D.1- The H+ or Na+-translocating NADH Dehyrogenase (NDH) Family3.D.9- The H+-translocating F420H2 Dehydrogenase (F420H2DH) Family Mrp of ''Bacillus subtilis'' is a 7 subunit Na+/H+ antiporter An antiporter (also called exchanger or counter-transporter) is a cotransporter and integral membrane protein involved in secondary active transport of two or more different molecules or ions across a phospholipid membrane such as the plasma membr ... comple(TC# 2.A.63.1.4) All subunits are homologous to the subunits in other members of this monovalent cation (K+ or Na+):proton antiporter-3 (CPA3) family as well as subunits in the archaeal hydrogenasesTC#s 3.D.1.4.1an3.D.1.4.2, which share several subunits with NADH dehydrogenase subunits (3.D.1). The largest subunits of the Mrp complex (MrpA ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Respiratory Complex I
Respiratory complex I, (also known as NADH:ubiquinone oxidoreductase, Type I NADH dehydrogenase and mitochondrial complex I) is the first large protein complex of the respiratory chains of many organisms from bacteria to humans. It catalyzes the transfer of electrons from NADH to coenzyme Q10 (CoQ10) and translocates protons across the inner mitochondrial membrane in eukaryotes or the plasma membrane of bacteria. This enzyme is essential for the normal functioning of cells, and mutations in its subunits lead to a wide range of inherited neuromuscular and metabolic disorders. Defects in this enzyme are responsible for the development of several pathological processes such as ischemia/reperfusion damage (stroke and cardiac infarction), Parkinson's disease and others. Function Complex I is the first enzyme of the mitochondrial electron transport chain. There are three energy-transducing enzymes in the electron transport chain - NADH:ubiquinone oxidoreductase (complex I ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
NADH Dehydrogenase
NADH dehydrogenase is an enzyme that converts nicotinamide adenine dinucleotide (NAD) from its reduced form (NADH) to its oxidized form (NAD+). Members of the NADH dehydrogenase family and analogues are commonly systematically named using the format ''NADH:acceptor oxidoreductase''. The chemical reaction these enzymes catalyze are generally represented with the follow equation; : NADH + H+ + acceptor NAD+ + reduced acceptor NADH dehydrogenase is a flavoprotein that contains iron-sulfur centers. NADH dehydrogenase is used in the electron transport chain for generation of ATP. The EC term NADH dehydrogenase (quinone) (EC 1.6.5.11) is defined for NADH dehydrogenases that use a quinone (excluding ubiquinone) as the acceptor. The EC term NADH dehydrogenase (ubiquinone) Respiratory complex I, (also known as NADH:ubiquinone oxidoreductase, Type I NADH dehydrogenase and mitochondrial complex I) is the first large protein complex of the respiratory chains of many organisms from ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Proton ATPase
In the field of enzymology, a proton ATPase is an enzyme that catalyzes the following chemical reaction: :ATP + + in \rightleftharpoons ADP + phosphate + out The 3 substrates of this enzyme are ATP, , and , whereas its 3 products are ADP, phosphate, and . Proton ATPases are divided into three groups as outlined below: P-type proton ATPase P-type ATPases form a covalent phosphorylated (hence the symbol ’P') intermediate as part of its reaction cycle. P-type ATPases undergo major conformational changes during the catalytic cycle. P-type ATPases are not evolutionary related to V- and F-type ATPases. Plasma membrane H+-ATPase P-type proton ATPase (or plasma membrane -ATPase) is found in the plasma membranes of eubacteria, archaea, protozoa, fungi and plants. Here it serves as a functional equivalent to the Na+/K+ ATPase of animal cells; i.e. it energizes the plasma membrane by forming an electrochemical gradient of protons (Na+ in animal cells), that in turn drives sec ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Adenosine Triphosphate
Adenosine triphosphate (ATP) is an organic compound that provides energy to drive many processes in living cells, such as muscle contraction, nerve impulse propagation, condensate dissolution, and chemical synthesis. Found in all known forms of life, ATP is often referred to as the "molecular unit of currency" of intracellular energy transfer. When consumed in metabolic processes, it converts either to adenosine diphosphate (ADP) or to adenosine monophosphate (AMP). Other processes regenerate ATP. The human body recycles its own body weight equivalent in ATP each day. It is also a precursor to DNA and RNA, and is used as a coenzyme. From the perspective of biochemistry, ATP is classified as a nucleoside triphosphate, which indicates that it consists of three components: a nitrogenous base ( adenine), the sugar ribose, and the triphosphate. Structure ATP consists of an adenine attached by the 9-nitrogen atom to the 1′ carbon atom of a sugar ( ribose), which in tu ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Proton-pumping Pyrophosphatase
Members of the H+, Na+-translocating Pyrophosphatase (M+''-PPase)'' FamilyTC# 3.A.10 are found in the vacuolar ( tonoplast) membranes of higher plants, algae, and protozoa, and in both bacteria and archaea. They are therefore ancient enzymes. Two types of inorganic diphosphatase, very different in terms of both amino acid sequence and structure, have been characterised to date: soluble and transmembrane proton-pumping pyrophosphatases (sPPases and H(+)-PPases, respectively). sPPases are ubiquitous proteins that hydrolyse pyrophosphate to release heat, whereas H+-PPases, so far unidentified in animal and fungal cells, couple the energy of PPi hydrolysis to proton movement across biological membranes. The latter type is represented by this group of proteins. H+-PPases vacuolar-type inorganic pyrophosphatases (V-PPase) or pyrophosphate-energised vacuolar membrane proton pumps. In plants, vacuoles contain two enzymes for acidifying the interior of the vacuole, the V-ATPase and the ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Pyrophosphate
In chemistry, pyrophosphates are phosphorus oxyanions that contain two phosphorus atoms in a P–O–P linkage. A number of pyrophosphate salts exist, such as disodium pyrophosphate (Na2H2P2O7) and tetrasodium pyrophosphate (Na4P2O7), among others. Often pyrophosphates are called diphosphates. The parent pyrophosphates are derived from partial or complete neutralization of pyrophosphoric acid. The pyrophosphate bond is also sometimes referred to as a phosphoanhydride bond, a naming convention which emphasizes the loss of water that occurs when two phosphates form a new P–O–P bond, and which mirrors the nomenclature for anhydrides of carboxylic acids. Pyrophosphates are found in ATP and other nucleotide triphosphates, which are important in biochemistry. The term pyrophosphate is also the name of esters formed by the condensation of a phosphorylated biological compound with inorganic phosphate, as for dimethylallyl pyrophosphate. This bond is also referred to as a high-ene ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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