1.
Photosynthesis
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Photosynthesis is a process used by plants and other organisms to convert light energy into chemical energy that can later be released to fuel the organisms activities. In most cases, oxygen is released as a waste product. Most plants, most algae, and cyanobacteria perform photosynthesis, such organisms are called photoautotrophs, in plants, these proteins are held inside organelles called chloroplasts, which are most abundant in leaf cells, while in bacteria they are embedded in the plasma membrane. In these light-dependent reactions, some energy is used to strip electrons from suitable substances, such as water, in the Calvin cycle, atmospheric carbon dioxide is incorporated into already existing organic carbon compounds, such as ribulose bisphosphate. Using the ATP and NADPH produced by the light-dependent reactions, the compounds are then reduced and removed to form further carbohydrates. Cyanobacteria appeared later, the oxygen they produced contributed directly to the oxygenation of the Earth. Today, the rate of energy capture by photosynthesis globally is approximately 130 terawatts. Photosynthetic organisms also convert around 100–115 thousand million tonnes of carbon into biomass per year. Photosynthetic organisms are photoautotrophs, which means that they are able to synthesize food directly from carbon dioxide, however, not all organisms that use light as a source of energy carry out photosynthesis, photoheterotrophs use organic compounds, rather than carbon dioxide, as a source of carbon. In plants, algae, and cyanobacteria, photosynthesis releases oxygen and this is called oxygenic photosynthesis and is by far the most common type of photosynthesis used by living organisms. Although there are differences between oxygenic photosynthesis in plants, algae, and cyanobacteria, the overall process is quite similar in these organisms. There are also varieties of anoxygenic photosynthesis, used mostly by certain types of bacteria. Carbon dioxide is converted into sugars in a process called carbon fixation, photosynthesis provides the energy in the form of free electrons that are used to split carbon from carbon dioxide that is then used to fix that carbon once again as carbohydrate. Carbon fixation is a redox reaction, so photosynthesis supplies the energy that drives both process. In the first stage, light-dependent reactions or light reactions capture the energy of light and use it to make the energy-storage molecules ATP, during the second stage, the light-independent reactions use these products to capture and reduce carbon dioxide. Most organisms that utilize oxygenic photosynthesis use visible light for the light-dependent reactions, some organisms employ even more radical variants of photosynthesis. Some archea use a method that employs a pigment similar to those used for vision in animals. The bacteriorhodopsin changes its configuration in response to sunlight, acting as a proton pump and this produces a proton gradient more directly, which is then converted to chemical energy
2.
Redox
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Redox is a chemical reaction in which the oxidation states of atoms are changed. Any such reaction involves both a process and a complementary oxidation process, two key concepts involved with electron transfer processes. Redox reactions include all chemical reactions in which atoms have their oxidation state changed, in general, the chemical species from which the electron is stripped is said to have been oxidized, while the chemical species to which the electron is added is said to have been reduced. It can be explained in terms, Oxidation is the loss of electrons or an increase in oxidation state by a molecule, atom. Reduction is the gain of electrons or a decrease in state by a molecule, atom. As an example, during the combustion of wood, oxygen from the air is reduced, the reaction can occur relatively slowly, as in the case of rust, or more quickly, as in the case of fire. Redox is a portmanteau of reduction and oxidation, the word oxidation originally implied reaction with oxygen to form an oxide, since dioxygen was historically the first recognized oxidizing agent. Later, the term was expanded to encompass oxygen-like substances that accomplished parallel chemical reactions, ultimately, the meaning was generalized to include all processes involving loss of electrons. The word reduction originally referred to the loss in weight upon heating a metallic ore such as an oxide to extract the metal. In other words, ore was reduced to metal, antoine Lavoisier showed that this loss of weight was due to the loss of oxygen as a gas. Later, scientists realized that the atom gains electrons in this process. The meaning of reduction then became generalized to all processes involving gain of electrons. Even though reduction seems counter-intuitive when speaking of the gain of electrons, it help to think of reduction as the loss of oxygen. Since electrons are charged, it is also helpful to think of this as reduction in electrical charge. The electrochemist John Bockris has used the words electronation and deelectronation to describe reduction and oxidation processes respectively when they occur at electrodes and these words are analogous to protonation and deprotonation, but they have not been widely adopted by chemists. The term hydrogenation could be used instead of reduction, since hydrogen is the agent in a large number of reactions. But, unlike oxidation, which has been generalized beyond its root element, the word redox was first used in 1928. The processes of oxidation and reduction occur simultaneously and cannot happen independently of one another, the oxidation alone and the reduction alone are each called a half-reaction, because two half-reactions always occur together to form a whole reaction
3.
Glycolysis
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Glycolysis is the metabolic pathway that converts glucose C6H12O6, into pyruvate, CH3COCOO− + H+. The free energy released in this process is used to form the high-energy molecules ATP, glycolysis is a determined sequence of ten enzyme-catalyzed reactions. The intermediates provide entry points to glycolysis, for example, most monosaccharides, such as fructose and galactose, can be converted to one of these intermediates. The intermediates may also be directly useful, for example, the intermediate dihydroxyacetone phosphate is a source of the glycerol that combines with fatty acids to form fat. Glycolysis is an oxygen independent metabolic pathway, meaning that it not use molecular oxygen for any of its reactions. However the products of glycolysis are sometimes metabolized using atmospheric oxygen, when molecular oxygen is used for the metabolism of the products of glycolysis the process is usually referred to as aerobic, whereas if no oxygen is used the process is said to be anaerobic. Thus, glycolysis occurs, with variations, in all organisms. The wide occurrence of glycolysis indicates that it is one of the most ancient metabolic pathways, glycolysis could thus have originated from chemical constraints of the prebiotic world. Glycolysis occurs in most organisms in the cytosol of the cell, the most common type of glycolysis is the Embden–Meyerhof–Parnas, which was discovered by Gustav Embden, Otto Meyerhof, and Jakub Karol Parnas. Glycolysis also refers to other pathways, such as the Entner–Doudoroff pathway, however, the discussion here will be limited to the Embden–Meyerhof–Parnas pathway. The overall reaction of glycolysis is, The use of symbols in this equation makes it appear unbalanced with respect to oxygen atoms, hydrogen atoms, and charges. In the cellular environment, all three groups of ADP dissociate into −O− and H+, giving ADP3−, and this ion tends to exist in an ionic bond with Mg2+. ATP behaves identically except that it has four groups, giving ATPMg2−. When these differences along with the charges on the two phosphate groups are considered together, the net charges of −4 on each side are balanced. For simple fermentations, the metabolism of one molecule of glucose to two molecules of pyruvate has a net yield of two molecules of ATP, most cells will then carry out further reactions to repay the used NAD+ and produce a final product of ethanol or lactic acid. Many bacteria use inorganic compounds as hydrogen acceptors to regenerate the NAD+, cells performing aerobic respiration synthesize much more ATP, but not as part of glycolysis. These further aerobic reactions use pyruvate and NADH + H+ from glycolysis, the pathway of glycolysis as it is known today took almost 100 years to fully discover. The combined results of many experiments were required in order to understand the pathway as a whole
4.
Phosphoglycerate kinase
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Phosphoglycerate kinase is an enzyme that catalyzes the reversible transfer of a phosphate group from 1, 3-bisphosphoglycerate to ADP producing 3-phosphoglycerate and ATP. Like all kinases it is a transferase, PGK is a major enzyme used in glycolysis, in the first ATP-generating step of the glycolytic pathway. In gluconeogenesis, the reaction catalyzed by PGK proceeds in the direction, generating ADP and 1. In humans, two isozymes of PGK have been so far identified, PGK1 and PGK2, PGK is present in all living organisms as one of the two ATP-generating enzymes in glycolysis. In the gluconeogenic pathway, PGK catalyzes the reverse reaction, under biochemical standard conditions, the glycolytic direction is favored. In the Calvin cycle in photosynthetic organisms, PGK catalyzes the phosphorylation of 3-PG, producing 1, 3-BPG and ADP, as part of the reactions that regenerate ribulose-1, 5-bisphosphate. PGK has been reported to exhibit thiol reductase activity on plasmin, leading to angiostatin formation, the enzyme was also shown to participate in DNA replication and repair in mammal cell nuclei. The human isozyme PGK2, which is expressed during spermatogenesis, was shown to be essential for sperm function in mice. Click on genes, proteins and metabolites below to link to respective articles, PGK is found in all living organisms and its sequence has been highly conserved throughout evolution. The enzyme exists as a 415-residue monomer containing two nearly equal-sized domains that correspond to the N- and C-termini of the protein, 3-phosphoglycerate binds to the N-terminal, while the nucleotide substrates, MgATP or MgADP, bind to the C-terminal domain of the enzyme. This extended two-domain structure is associated with large-scale hinge-bending conformational changes, the two domains of the protein are separated by a cleft and linked by two alpha-helices. At the core of each domain is a 6-stranded parallel beta-sheet surrounded by alpha helices, the two lobes are capable of folding independently, consistent with the presence of intermediates on the folding pathway with a single domain folded. Though the binding of either substrate triggers a change, only through the binding of both substrates does domain closure occur, leading to the transfer of the phosphate group. Magnesium ions are complexed to the phosphate groups the nucleotide substrates of PGK. It is known that in the absence of magnesium, no enzyme activity occurs and it is theorized that the ion may also encourage domain closure when PGK has bound both substrates. Without either substrate bound, PGK exists in an open conformation, then, in the case of the forward glycolytic reaction, the beta-phosphate of ADP initiates a nucleophilic attack on the 1-phosphate of 1, 3-BPG. The Lys219 on the enzyme guides the group to the substrate. In the glycolytic pathyway,1, 3-BPG is the donor and has a high phosphoryl-transfer potential
5.
Hexokinase
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A hexokinase is an enzyme that phosphorylates hexoses, forming hexose phosphate. In most organisms, glucose is the most important substrate of hexokinases, scientists have discovered and demonstrated that Hexokinase posses the ability to transfer a inorganic phosphate group from ATP to a substrate. Hexokinases should not be confused with glucokinase, which is an isoform of hexokinase. While other hexokinases are capable of phosphorylating several hexoses, glucokinase acts with a 50-fold lower substrate affinity and its only hexose substrate is glucose. Genes that encode hexokinase have been discovered in every domain of life, and exist among a variety of species range from bacteria, yeast. They are categorized as actin fold proteins, sharing a common ATP binding site core that is surrounded by more variable sequences which determine substrate affinities, several hexokinase isoforms or isozymes that provide different functions can occur in a single species. Phosphorylation of a such as glucose often limits it to a number of intracellular metabolic processes. This is because phosphorylated hexoses are charged, and thus difficult to transport out of a cell. Most bacterial hexokinases are approximately 50 kD in size, multicellular organisms including plants and animals often have more than one hexokinase isoform. Most are about 100 kD in size and consist of two halves, which share much sequence homology and this suggests an evolutionary origin by duplication and fusion of a 50kD ancestral hexokinase similar to those of bacteria. There are four important mammalian hexokinase isozymes that vary in subcellular locations and kinetics with respect to different substrates and conditions, and physiological function. They are designated hexokinases I, II, III, and IV or hexokinases A, B, C, and D. Hexokinases I, II, Hexokinases I and II follow Michaelis-Menten kinetics at physiologic concentrations of substrates. All three are strongly inhibited by their product, glucose-6-phosphate, molecular weights are around 100 kD. Each consists of two similar 50kD halves, but only in hexokinase II do both halves have functional active sites, Hexokinase I/A is found in all mammalian tissues, and is considered a housekeeping enzyme, unaffected by most physiological, hormonal, and metabolic changes. Hexokinase II/B constitutes the principal regulated isoform in many types and is increased in many cancers. It is the hexokinase found in muscle and heart, Hexokinase II is also located at the mitochondria outer membrane so it can have direct access to ATP. Hexokinase III/C is substrate-inhibited by glucose at physiologic concentrations, little is known about the regulatory characteristics of this isoform. Mammalian hexokinase IV, also referred to as glucokinase, differs from other hexokinases in kinetics, the location of the phosphorylation on a subcellular level occurs when glucokinase translocates between the cytoplasm and nucleus of liver cells
6.
Conjugate acid
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A conjugate acid, within the Brønsted–Lowry acid–base theory, is a species formed by the reception of a proton by a base—in other words, it is a base with a hydrogen ion added to it. On the other hand, a base is merely what is left after an acid has donated a proton in a chemical reaction. Hence, a base is a species formed by the removal of a proton from an acid. A proton is a particle with a unit positive electrical charge, it is represented by the symbol H+ because it constitutes the nucleus of a hydrogen atom, that is. A cation can be an acid, and an anion can be a conjugate base, depending on which substance is involved. In an acid-base reaction, an acid plus a base reacts to form a conjugate base plus a conjugate acid, refer to the following figure, We say that the water molecule is the conjugate acid of the hydroxide ion after the latter received the hydrogen proton donated by ammonium. On the other hand, ammonia is the base for the acid ammonium after ammonium has donated a hydrogen ion towards the production of the water molecule. The strength of an acid is directly proportional to its dissociation constant. If a conjugate acid is strong, its dissociation will have an equilibrium constant. The strength of a base can be seen as the tendency of the species to pull hydrogen protons towards itself. If a conjugate base is classified as strong, it will hold on to the hydrogen proton when in solution, if a chemical species is classified as a weak acid, its conjugate base will be strong in nature. This can be observed in ammonias reaction with water, the reaction proceeds until most of the ammonia has been transformed to ammonium. This shift to the right in the equilibrium of the reaction means that ammonium does not dissociate easily in water. On the other hand, if a species is classified as a strong acid, an example of this case would be the dissociation of Hydrochloric acid HCl in water. Since HCl is an acid, its conjugate base will be a weak conjugate base. Therefore, in system, most H+ will be in the form of a Hydronium ion H 3O+ instead of attached to a Cl anion. To summarize, the stronger the acid or base, the weaker the conjugate, the acid and conjugate base as well as the base and conjugate acid are known as conjugate pairs. When finding a conjugate acid or base, it is important to look at the reactants of the chemical equation, to identify the conjugate acid, look for the pair of compounds that are related
7.
Jmol
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Jmol is computer software for molecular modelling chemical structures in 3-dimensions. Jmol returns a 3D representation of a molecule that may be used as a teaching tool and it is written in the programming language Java, so it can run on the operating systems Windows, macOS, Linux, and Unix, if Java is installed. It is free and open-source software released under a GNU Lesser General Public License version 2.0, a standalone application and a software development kit exist that can be integrated into other Java applications, such as Bioclipse and Taverna. A popular feature is an applet that can be integrated into web pages to display molecules in a variety of ways, for example, molecules can be displayed as ball-and-stick models, space-filling models, ribbon diagrams, etc. Jmol supports a range of chemical file formats, including Protein Data Bank, Crystallographic Information File, MDL Molfile. There is also a JavaScript-only version, JSmol, that can be used on computers with no Java, the Jmol applet, among other abilities, offers an alternative to the Chime plug-in, which is no longer under active development. While Jmol has many features that Chime lacks, it does not claim to reproduce all Chime functions, most notably, Chime requires plug-in installation and Internet Explorer 6.0 or Firefox 2.0 on Microsoft Windows, or Netscape Communicator 4.8 on Mac OS9. Jmol requires Java installation and operates on a variety of platforms. For example, Jmol is fully functional in Mozilla Firefox, Internet Explorer, Opera, Google Chrome, fast and Scriptable Molecular Graphics in Web Browsers without Java3D
8.
Catalysis
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Catalysis is the increase in the rate of a chemical reaction due to the participation of an additional substance called a catalyst. In most cases, reactions occur faster with a catalyst because they require less activation energy, furthermore, since they are not consumed in the catalyzed reaction, catalysts can continue to act repeatedly. Often only tiny amounts are required in principle, in the presence of a catalyst, less free energy is required to reach the transition state, but the total free energy from reactants to products does not change. A catalyst may participate in multiple chemical transformations, the effect of a catalyst may vary due to the presence of other substances known as inhibitors or poisons or promoters. Catalyzed reactions have an activation energy than the corresponding uncatalyzed reaction, resulting in a higher reaction rate at the same temperature. However, the mechanics of catalysis is complex. Usually, the catalyst participates in this slowest step, and rates are limited by amount of catalyst, in heterogeneous catalysis, the diffusion of reagents to the surface and diffusion of products from the surface can be rate determining. A nanomaterial-based catalyst is an example of a heterogeneous catalyst, analogous events associated with substrate binding and product dissociation apply to homogeneous catalysts. Although catalysts are not consumed by the reaction itself, they may be inhibited, deactivated, in heterogeneous catalysis, typical secondary processes include coking where the catalyst becomes covered by polymeric side products. Additionally, heterogeneous catalysts can dissolve into the solution in a system or sublimate in a solid–gas system. The production of most industrially important chemicals involves catalysis, similarly, most biochemically significant processes are catalysed. Research into catalysis is a field in applied science and involves many areas of chemistry, notably organometallic chemistry. Catalysis is relevant to aspects of environmental science, e. g. the catalytic converter in automobiles. Many transition metals and transition metal complexes are used in catalysis as well, Catalysts called enzymes are important in biology. A catalyst works by providing a reaction pathway to the reaction product. The rate of the reaction is increased as this route has a lower activation energy than the reaction route not mediated by the catalyst. The disproportionation of hydrogen peroxide creates water and oxygen, as shown below,2 H2O2 →2 H2O + O2 This reaction is preferable in the sense that the reaction products are more stable than the starting material, though the uncatalysed reaction is slow. In fact, the decomposition of hydrogen peroxide is so slow that hydrogen peroxide solutions are commercially available and this reaction is strongly affected by catalysts such as manganese dioxide, or the enzyme peroxidase in organisms
9.
Glyceraldehyde 3-phosphate dehydrogenase
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Glyceraldehyde 3-phosphate dehydrogenase is an enzyme of ~37kDa that catalyzes the sixth step of glycolysis and thus serves to break down glucose for energy and carbon molecules. In sperm, a testis-specific isoenzyme GAPDHS is expressed, under normal cellular conditions, cytoplasmic GAPDH exists primarily as a tetramer. This form is composed of four identical 37-kDa subunits containing a single catalytic thiol group each, nuclear GAPDH has increased isoelectric point of pH8. 3–8.7. Of note, the cysteine residue C152 in the active site is required for the induction of apoptosis by oxidative stress. Notably, post-translational modifications of cytoplasmic GAPDH contribute to its functions outside of glycolysis, compound C00118 at KEGG Pathway Database. Enzyme 1.2.1.12 at KEGG Pathway Database, reaction R01063 at KEGG Pathway Database. Compound C00236 at KEGG Pathway Database and this is an example of phosphorylation coupled to oxidation, and the overall reaction is somewhat endergonic. Energy coupling here is possible by GAPDH. GAPDH uses covalent catalysis and general base catalysis to decrease the very large, first, a cysteine residue in the active site of GAPDH attacks the carbonyl group of GAP, creating a hemithioacetal intermediate. Next, an adjacent, tightly bound molecule of NAD+ accepts a hydride ion from GAP, forming NADH and this thioester species is much higher in energy than the carboxylic acid species that would result in the absence of GAPDH. Donation of the ion by the hemithioacetal is facilitated by its deprotonation by a histidine residue in the enzymes active site. Deprotonation encourages the reformation of the group in the thioester intermediate. This protein may use the model of allosteric regulation. As its name indicates, glyceraldehyde 3-phosphate dehydrogenase catalyses the conversion of glyceraldehyde 3-phosphate to D-glycerate 1 and this is the 6th step in the glycolytic breakdown of glucose, an important pathway of energy and carbon molecule supply which takes place in the cytosol of eukaryotic cells. The conversion occurs in two coupled steps, the first is favourable and allows the second unfavourable step to occur. The OCA-S transcriptional coactivator complex contains GAPDH and lactate dehydrogenase, two proteins previously thought to be involved in metabolism. GAPDH moves between the cytosol and the nucleus and may link the metabolic state to gene transcription. In 2005, Hara et al. showed that GAPDH initiates apoptosis and this is not a third function, but can be seen as an activity mediated by GAPDH binding to DNA like in transcription activation, discussed above
10.
Dihydrolipoyl transacetylase
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Dihydrolipoyl transacetylase is an enzyme component of the multienzyme pyruvate dehydrogenase complex. The pyruvate dehydrogenase complex is responsible for the decarboxylation step that links glycolysis to the citric acid cycle. This involves the transformation of pyruvate from glycolysis into acetyl-CoA which is used in the citric acid cycle to carry out cellular respiration. There are three different enzyme components in the pyruvate dehydrogenase complex, pyruvate dehydrogenase is responsible for the oxidation of pyruvate, dihydrolipoyl transacetylase transfers the acetyl group to coenzyme A, and dihydrolipoyl dehydrogenase regenerates the lipoamide. In humans, dihydrolipoyl transacetylase enzymatic activity resides in the pyruvate dehydrogenase complex component E2 that is encoded by the DLAT gene, the systematic name of this enzyme class is acetyl-CoA, enzyme N6-lysine S-acetyltransferase. Other names in use include, All dihydrolipoyl transacetylases have a unique multidomain structure consisting of,3 lipoyl domains, an interaction domain. Interestingly all the domains are connected by disordered, low complexity linker regions, depending on the species, multiple subunits of dihydrolipoyl transacetylase enzymes can arrange together into either a cubic or dodecahedral shape. The cubic core structure, found in such as Azotobacter vinelandii, is made up of 24 subunits total. The catalytic domains are assembled into trimers with the site located at the subunit interface. The topology of this active site is identical to that of chloramphenicol acetyltransferase. Eight of these trimers are then arranged into a truncated cube. The two main substrates, CoA and the lipoamide, are found at two opposite entrances of a 30 Å long channel which runs between the subunits and forms the catalytic center, CoA enters from the inside of the cube, and the lipoamide enters from the outside. The subunits are arranged in sets of three, similar to the trimers in the cubic shape, with each set making up one of the 20 dodecahedral vertices. Dihydrolipoyl transacetylase participates in the decarboxylation reaction that links glycolysis to the citric acid cycle. The various parts of cellular respiration take place in different parts of the cell, thus pyruvate dehydrogenase complexes are found in the mitochondria of eukaryotes. Pyruvate decarboxylation requires a few cofactors in addition to the enzymes that make up the complex, the first is thiamine pyrophosphate, which is used by pyruvate dehydrogenase to oxidize pyruvate and to form a hydroxyethyl-TPP intermediate. This intermediate is taken up by dihydrolipoyl transacetylase and reacted with a second lipoamide cofactor to generate an acetyl-dihydrolipoyl intermediate and this second intermediate can then be attacked by the nucleophilic sulfur attached to Coenzyme A, and the dihydrolipoamide is released. This results in the production of acetyl CoA, which is the end goal of pyruvate decarboxylation, the dihydrolipoamide is taken up by dihydrolipoyl dehydrogenase, and with the additional cofactors FAD and NAD+, regenerates the original lipoamide
11.
2,3-Bisphosphoglyceric acid
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2, 3-Bisphosphoglyceric acid, also known as 2, 3-diphosphoglyceric acid, is a three-carbon isomer of the glycolytic intermediate 1, 3-bisphosphoglyceric acid. 2, 3-BPG is present in red blood cells at approximately 5 mmol/L. 2, 3-BPG is thus an allosteric effector and its function was discovered in 1967 by Reinhold Benesch and Ruth Benesch. 2, 3-BPG is formed from 1, 3-BPG by the enzyme BPG mutase and it can then be broken down by 2, 3-BPG phosphatase to form 3-phosphoglycerate. 2, 3-BPG, the most concentrated organophosphate in the erythrocyte, the concentration of 2, 3-BPG varies proportionately to the, which is inhibitory to catalytic action of bisphosphoglycerate phosphatase. There is a balance between the need to generate ATP to support energy requirements for cell metabolism and the need to maintain appropriate oxygenation/deoxygenation status of hemoglobin. This balance is maintained by isomerisation of 1, 3-BPG to 2, 3-BPG, low pH activates the activity of biphosphoglyceromutase and inhibits bisphosphoglyerate phosphatase, which leads to increases in 2, 3-BPG. When 2, 3-BPG binds to deoxyhemoglobin, it acts to stabilize the low affinity state of the oxygen carrier. The R state, with oxygen bound to a group, has a different conformation. By itself, hemoglobin has sigmoid-like kinetics, in selectively binding to deoxyhemoglobin,2, 3-BPG stabilizes the T state conformation, making it harder for oxygen to bind hemoglobin and more likely to be released to adjacent tissues. 2, 3-BPG is part of a loop that can help prevent tissue hypoxia in conditions where it is most likely to occur. Ultimately, this mechanism increases oxygen release from RBCs under circumstances where it is needed most and this release is potentiated by the Bohr effect in tissues with high energetic demands. Bohr effect is another way to solve the affinity problem of the hemoglobin, and it is related to the pH. It’s important to highlight that the behaviour of myoglobin doesn’t work in the way, as 2. In pregnant women, there is a 30% increase in intracellular 2 and this lowers the maternal hemoglobin affinity for oxygen, and therefore allows more oxygen to be offloaded to the fetus in the maternal uterine arteries. The foetus has a low sensitivity to 2, 3-BPG, so its hemoglobin has an affinity for oxygen. Therefore although the pO2 in the arteries is low, the foetal umbilical arteries can still get oxygenated from them. It is interesting to note that fetal hemoglobin exhibits a low affinity for 2, 3-BPG and this increased oxygen-binding affinity relative to that of adult hemoglobin is due to HbFs having two α/γ dimers as opposed to the two α/β dimers of HbA
12.
Nicotinamide adenine dinucleotide
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Nicotinamide adenine dinucleotide is a coenzyme found in all living cells. The compound is a dinucleotide, because it consists of two nucleotides joined through their phosphate groups, one nucleotide contains an adenine base and the other nicotinamide. Nicotinamide adenine dinucleotide exists in two forms, an oxidized and reduced form abbreviated as NAD+ and NADH respectively, in metabolism, nicotinamide adenine dinucleotide is involved in redox reactions, carrying electrons from one reaction to another. The coenzyme is, therefore, found in two forms in cells, NAD+ is an oxidizing agent – it accepts electrons from other molecules and becomes reduced and this reaction forms NADH, which can then be used as a reducing agent to donate electrons. These electron transfer reactions are the function of NAD. However, it is used in other cellular processes, the most notable one being a substrate of enzymes that add or remove chemical groups from proteins. Because of the importance of these functions, the involved in NAD metabolism are targets for drug discovery. In organisms, NAD can be synthesized from simple building-blocks from the amino acids tryptophan or aspartic acid, in an alternative fashion, more complex components of the coenzymes are taken up from food as the vitamin called niacin. Similar compounds are released by reactions that break down the structure of NAD and these preformed components then pass through a salvage pathway that recycles them back into the active form. Some NAD is also converted into nicotinamide adenine dinucleotide phosphate, the chemistry of this related coenzyme is similar to that of NAD, nicotinamide adenine dinucleotide, like all dinucleotides, consists of two nucleosides joined by a pair of bridging phosphate groups. The nucleosides each contain a ring, one with adenine attached to the first carbon atom. The nicotinamide moiety can be attached in two orientations to this carbon atom. Because of these two structures, the compound exists as two diastereomers. It is the diastereomer of NAD+ that is found in organisms. These nucleotides are joined together by a bridge of two groups through the 5 carbons. In metabolism, the compound accepts or donates electrons in redox reactions, such reactions involve the removal of two hydrogen atoms from the reactant, in the form of a hydride ion, and a proton. The proton is released into solution, while the reductant RH2 is oxidized, the midpoint potential of the NAD+/NADH redox pair is −0.32 volts, which makes NADH a strong reducing agent. The reaction is reversible, when NADH reduces another molecule and is re-oxidized to NAD+
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