A peroxisome is a type of organelle known as a microbody, found in all eukaryotic cells. They are involved in catabolism of long chain fatty acids, branched chain fatty acids, D-amino acids, polyamines, reduction of reactive oxygen species – hydrogen peroxide – and biosynthesis of plasmalogens, i.e. ether phospholipids critical for the normal function of mammalian brains and lungs. They contain 10% of the total activity of two enzymes in the pentose phosphate pathway, important for energy metabolism, it is vigorously debated whether peroxisomes are involved in isoprenoid and cholesterol synthesis in animals. Other known peroxisomal functions include the glyoxylate cycle in germinating seeds, photorespiration in leaves, glycolysis in trypanosomes, methanol and/or amine oxidation and assimilation in some yeasts. Peroxisomes were identified as organelles by the Belgian cytologist Christian de Duve in 1967 after they had been first described by a Swedish doctoral student, J. Rhodin in 1954. A major function of the peroxisome is the breakdown of long chain fatty acids through beta oxidation.
In animal cells, the long fatty acids are converted to medium chain fatty acids, which are subsequently shuttled to mitochondria where they are broken down to carbon dioxide and water. In yeast and plant cells, this process is carried out in peroxisomes; the first reactions in the formation of plasmalogen in animal cells occur in peroxisomes. Plasmalogen is the most abundant phospholipid in myelin. Deficiency of plasmalogens causes profound abnormalities in the myelination of nerve cells, one reason why many peroxisomal disorders affect the nervous system. Peroxisomes play a role in the production of bile acids important for the absorption of fats and fat-soluble vitamins, such as vitamins A and K. Skin disorders are features of genetic disorders affecting peroxisome function as a result. Peroxisomes contain oxidative enzymes, such as uric acid oxidase; however the last enzyme is absent in humans, explaining the disease known as gout, caused by the accumulation of uric acid. Certain enzymes within the peroxisome, by using molecular oxygen, remove hydrogen atoms from specific organic substrates, in an oxidative reaction, producing hydrogen peroxide: R H 2 + O 2 → R + H 2 O 2 Catalase, another peroxisomal enzyme, uses this H2O2 to oxidize other substrates, including phenols, formic acid and alcohol, by means of the peroxidation reaction: H 2 O 2 + R ′ H 2 → R ′ + 2 H 2 O, thus eliminating the poisonous hydrogen peroxide in the process.
This reaction is important in liver and kidney cells, where the peroxisomes detoxify various toxic substances that enter the blood. About 25% of the ethanol alcohol humans drink is oxidized to acetaldehyde in this way. In addition, when excess H2O2 accumulates in the cell, catalase converts it to H2O through this reaction: 2 H 2 O 2 → 2 H 2 O + O 2 In higher plants, peroxisomes contain a complex battery of antioxidative enzymes such as superoxide dismutase, the components of the ascorbate-glutathione cycle, the NADP-dehydrogenases of the pentose-phosphate pathway, it has been demonstrated that peroxisomes generate nitric oxide radicals. The peroxisome of plant cells is polarised. Infection causes a glucosinolate molecule to play an antifungal role to be made and delivered to the outside of the cell through the action of the peroxisomal proteins. Peroxisomes can be replicate by fission. Peroxisome matrix proteins are translated in the cytoplasm prior to import. Specific amino acid sequences at the C-terminus or N-terminus of peroxisomal matrix proteins signals them to be imported into the organelle.
There are at least 32 known peroxisomal proteins, called peroxins, which participate in the process of peroxisome assembly. Proteins do not have to unfold to be imported into the peroxisome; the protein receptors, the peroxins PEX5 and PEX7, accompany their cargoes all the way into the peroxisome where they release the cargo and return to the cytosol – a step named recycling. A model describing the import cycle is referred to as the extended shuttle mechanism. There is now evidence. Ubiquitination appears to be crucial for the export of PEX5 from the peroxisome, to the cytosol. Peroxisomal disorders are a class of medical conditions that affect the human nervous system as well as many other organ systems. Two common examples are X-linked peroxisome biogenesis disorders. PEX genes encode the protein machinery required for proper perox
Red blood cell
Red blood cells known as RBCs, red cells, red blood corpuscles, erythroid cells or erythrocytes, are the most common type of blood cell and the vertebrate's principal means of delivering oxygen to the body tissues—via blood flow through the circulatory system. RBCs take up oxygen in the lungs, or gills of fish, release it into tissues while squeezing through the body's capillaries; the cytoplasm of erythrocytes is rich in hemoglobin, an iron-containing biomolecule that can bind oxygen and is responsible for the red color of the cells and the blood. The cell membrane is composed of proteins and lipids, this structure provides properties essential for physiological cell function such as deformability and stability while traversing the circulatory system and the capillary network. In humans, mature red blood cells are oval biconcave disks, they lack most organelles, in order to accommodate maximum space for hemoglobin. 2.4 million new erythrocytes are produced per second in human adults. The cells develop in the bone marrow and circulate for about 100–120 days in the body before their components are recycled by macrophages.
Each circulation takes about 60 seconds. A quarter of the cells in the human body are red blood cells. Nearly half of the blood's volume is red blood cells. Packed red blood cells are red blood cells that have been donated and stored in a blood bank for blood transfusion. All vertebrates, including all mammals and humans, have red blood cells. Red blood cells are cells present in blood; the only known vertebrates without red blood cells are the crocodile icefish. While they no longer use hemoglobin, remnants of hemoglobin genes can be found in their genome. Vertebrate red blood cells consist of hemoglobin, a complex metalloprotein containing heme groups whose iron atoms temporarily bind to oxygen molecules in the lungs or gills and release them throughout the body. Oxygen can diffuse through the red blood cell's cell membrane. Hemoglobin in the red blood cells carries some of the waste product carbon dioxide back from the tissues. Myoglobin, a compound related to hemoglobin, acts to store oxygen in muscle cells.
The color of red blood cells is due to the heme group of hemoglobin. The blood plasma alone is straw-colored, but the red blood cells change color depending on the state of the hemoglobin: when combined with oxygen the resulting oxyhemoglobin is scarlet, when oxygen has been released the resulting deoxyhemoglobin is of a dark red burgundy color. However, blood can appear bluish when seen through skin. Pulse oximetry takes advantage of the hemoglobin color change to directly measure the arterial blood oxygen saturation using colorimetric techniques. Hemoglobin has a high affinity for carbon monoxide, forming carboxyhemoglobin, a bright red in color. Flushed, confused patients with a saturation reading of 100% on pulse oximetry are sometimes found to be suffering from carbon monoxide poisoning. Having oxygen-carrying proteins inside specialized cells was an important step in the evolution of vertebrates as it allows for less viscous blood, higher concentrations of oxygen, better diffusion of oxygen from the blood to the tissues.
The size of red blood cells varies among vertebrate species. The red blood cells of mammals are shaped as biconcave disks: flattened and depressed in the center, with a dumbbell-shaped cross section, a torus-shaped rim on the edge of the disk; this shape allows for a high surface-area-to-volume ratio to facilitate diffusion of gases. However, there are some exceptions concerning shape in the artiodactyl order, which displays a wide variety of bizarre red blood cell morphologies: small and ovaloid cells in llamas and camels, tiny spherical cells in mouse deer, cells which assume fusiform, lanceolate and irregularly polygonal and other angular forms in red deer and wapiti. Members of this order have evolved a mode of red blood cell development different from the mammalian norm. Overall, mammalian red blood cells are remarkably flexible and deformable so as to squeeze through tiny capillaries, as well as to maximize their apposing surface by assuming a cigar shape, where they efficiently release their oxygen load.
Red blood cells in mammals are unique amongst vertebrates. Red blood cells of mammals cells have nuclei during early phases of erythropoiesis, but extrude them during development as they mature; the red blood cells without nuclei, called reticulocytes, subsequently lose all other cellular organelles such as their mitochondria, Golgi apparatus and endoplasmic reticulum. The spleen acts as a reservoir of red blood cells. In some other mammals such as dogs and horses, the spl
Pentose phosphate pathway
The pentose phosphate pathway is a metabolic pathway parallel to glycolysis. It generates NADPH and pentoses as well as ribose 5-phosphate, the last one a precursor for the synthesis of nucleotides. While it does involve oxidation of glucose, its primary role is anabolic rather than catabolic; the pathway is important in red blood cells. There are two distinct phases in the pathway; the first is the oxidative phase, in which NADPH is generated, the second is the non-oxidative synthesis of 5-carbon sugars. For most organisms, the pentose phosphate pathway takes place in the cytosol. Similar to glycolysis, the pentose phosphate pathway appears to have a ancient evolutionary origin; the reactions of this pathway are enzyme-catalyzed in modern cells, they occur non-enzymatically under conditions that replicate those of the Archean ocean, are catalyzed by metal ions ferrous ions. This suggests; the primary results of the pathway are: The generation of reducing equivalents, in the form of NADPH, used in reductive biosynthesis reactions within cells.
Production of ribose 5-phosphate, used in the synthesis of nucleic acids. Production of erythrose 4-phosphate used in the synthesis of aromatic amino acids. Aromatic amino acids, in turn, are precursors for many biosynthetic pathways, including the lignin in wood. Dietary pentose sugars derived from the digestion of nucleic acids may be metabolized through the pentose phosphate pathway, the carbon skeletons of dietary carbohydrates may be converted into glycolytic/gluconeogenic intermediates. In mammals, the PPP occurs in the cytoplasm, is found to be most active in the liver, mammary gland and adrenal cortex in the human; the PPP is one of the three main ways the body creates molecules with reducing power, accounting for 60% of NADPH production in humans. One of the uses of NADPH in the cell is to prevent oxidative stress, it reduces glutathione via glutathione reductase, which converts reactive H2O2 into H2O by glutathione peroxidase. If absent, the H2O2 would be converted to hydroxyl free radicals by Fenton chemistry, which can attack the cell.
Erythrocytes, for example, generate a large amount of NADPH through the pentose phosphate pathway to use in the reduction of glutathione. Hydrogen peroxide is generated for phagocytes in a process referred to as a respiratory burst. In this phase, two molecules of NADP+ are reduced to NADPH, utilizing the energy from the conversion of glucose-6-phosphate into ribulose 5-phosphate; the entire set of reactions can be summarized as follows: The overall reaction for this process is: Glucose 6-phosphate + 2 NADP+ + H2O → ribulose 5-phosphate + 2 NADPH + 2 H+ + CO2 Net reaction: 3 ribulose-5-phosphate → 1 ribose-5-phosphate + 2 xylulose-5-phosphate → 2 fructose-6-phosphate + glyceraldehyde-3-phosphate Glucose-6-phosphate dehydrogenase is the rate-controlling enzyme of this pathway. It is allosterically stimulated by NADP+ and inhibited by NADPH; the ratio of NADPH:NADP+ is about 100:1 in liver cytosol. This makes the cytosol a highly-reducing environment. An NADPH-utilizing pathway forms NADP+, which stimulates Glucose-6-phosphate dehydrogenase to produce more NADPH.
This step is inhibited by acetyl CoA. G6PD activity is post-translationally regulated by cytoplasmic deacetylase SIRT2. SIRT2-mediated deacetylation and activation of G6PD stimulates oxidative branch of PPP to supply cytosolic NADPH to counteract oxidative damage or support de novo lipogenesis. Several deficiencies in the level of activity of glucose-6-phosphate dehydrogenase have been observed to be associated with resistance to the malarial parasite Plasmodium falciparum among individuals of Mediterranean and African descent; the basis for this resistance may be a weakening of the red cell membrane such that it cannot sustain the parasitic life cycle long enough for productive growth. G6PD deficiency – A hereditary disease that disrupts the pentose phosphate pathway RNA Thiamine deficiency Frank Dickens FRS The chemical logic behind the pentose phosphate pathway Pentose+Phosphate+Pathway at the US National Library of Medicine Medical Subject Headings Pentose phosphate pathway Map – Homo sapiens
In biochemistry, a protein dimer is a macromolecular complex formed by two protein monomers, or single proteins, which are non-covalently bound. Many macromolecules, such as proteins or nucleic acids, form dimers; the word dimer has roots meaning "two parts", di- + -mer. A protein dimer is a type of protein quaternary structure. A protein homodimer is formed by two identical proteins. A protein heterodimer is formed by two different proteins. Most protein dimers in biochemistry are not connected by covalent bonds. An example of a non-covalent heterodimer is the enzyme reverse transcriptase, composed of two different amino acid chains. An exception is dimers that are linked by disulfide bridges such as the homodimeric protein NEMO; some proteins contain specialized domains to ensure specificity. Antibodies Receptor tyrosine kinases Transcription factors Leucine zipper motif proteins Nuclear receptors 14-3-3 proteins G protein-coupled receptors G protein βγ-subunit dimer Kinesin Triosephosphateisomerase Alcohol dehydrogenase Factor XI Factor XIII Toll-like receptor Fibrinogen Variable surface glycoproteins of the Trypanosoma parasite Tubulin Type II restriction enzymes Dimer Protein trimer Oligomer ProtCID
Protein Data Bank
The Protein Data Bank is a database for the three-dimensional structural data of large biological molecules, such as proteins and nucleic acids. The data obtained by X-ray crystallography, NMR spectroscopy, or cryo-electron microscopy, submitted by biologists and biochemists from around the world, are accessible on the Internet via the websites of its member organisations; the PDB is overseen by an organization called the Worldwide Protein Data Bank, wwPDB. The PDB is a key in areas such as structural genomics. Most major scientific journals, some funding agencies, now require scientists to submit their structure data to the PDB. Many other databases use protein structures deposited in the PDB. For example, SCOP and CATH classify protein structures, while PDBsum provides a graphic overview of PDB entries using information from other sources, such as Gene ontology. Two forces converged to initiate the PDB: 1) a small but growing collection of sets of protein structure data determined by X-ray diffraction.
In 1969, with the sponsorship of Walter Hamilton at the Brookhaven National Laboratory, Edgar Meyer began to write software to store atomic coordinate files in a common format to make them available for geometric and graphical evaluation. By 1971, one of Meyer's programs, SEARCH, enabled researchers to remotely access information from the database to study protein structures offline. SEARCH was instrumental in enabling networking, thus marking the functional beginning of the PDB; the Protein Data Bank was announced in October 1971 in Nature New Biology as a joint venture between Cambridge Crystallographic Data Centre, UK and Brookhaven National Laboratory, USA. Upon Hamilton's death in 1973, Tom Koeztle took over direction of the PDB for the subsequent 20 years. In January 1994, Joel Sussman of Israel's Weizmann Institute of Science was appointed head of the PDB. In October 1998, the PDB was transferred to the Research Collaboratory for Structural Bioinformatics; the new director was Helen M. Berman of Rutgers University.
In 2003, with the formation of the wwPDB, the PDB became an international organization. The founding members are PDBe, RCSB, PDBj; the BMRB joined in 2006. Each of the four members of wwPDB can act as deposition, data processing and distribution centers for PDB data; the data processing refers to the fact that annotate each submitted entry. The data are automatically checked for plausibility; the PDB database is updated weekly. The PDB holdings list is updated weekly; as of 17 October 2018, the breakdown of current holdings is as follows: 120,052 structures in the PDB have a structure factor file. 9,734 structures have an NMR restraint file. 3,486 structures in the PDB have a chemical shifts file. 2,531 structures in the PDB have a 3DEM map file deposited in EM Data BankThese data show that most structures are determined by X-ray diffraction, but about 10% of structures are now determined by protein NMR. When using X-ray diffraction, approximations of the coordinates of the atoms of the protein are obtained, whereas estimations of the distances between pairs of atoms of the protein are found through NMR experiments.
Therefore, the final conformation of the protein is obtained, in the latter case, by solving a distance geometry problem. A few proteins are determined by cryo-electron microscopy; the significance of the structure factor files, mentioned above, is that, for PDB structures determined by X-ray diffraction that have a structure file, the electron density map may be viewed. The data of such structures is stored on the "electron density server". In the past, the number of structures in the PDB has grown at an exponential rate, passing the 100 registered structures milestone in 1982, the 1,000 in 1993, the 10,000 in 1999, the 100,000 in 2014. However, since 2007, the rate of accumulation of new protein structures appears to have plateaued; the file format used by the PDB was called the PDB file format. This original format was restricted by the width of computer punch cards to 80 characters per line. Around 1996, the "macromolecular Crystallographic Information file" format, mmCIF, an extension of the CIF format started to be phased in.
MmCIF is now the master format for the PDB archive. An XML version of this format, called PDBML, was described in 2005; the structure files can be downloaded in any of these three formats. In fact, individual files are downloaded into graphics packages using web addresses: For PDB format files, use, e.g. http://www.pdb.org/pdb/files/4hhb.pdb.gz or http://pdbe.org/download/4hhb For PDBML files, use, e.g. http://www.pdb.org/pdb/files/4hhb.xml.gz or http://pdbe.org/pdbml/4hhbThe "4hhb" is the PDB identifier. Each structure published in PDB receives a four-character alphanumeric identifier, its PDB ID; the structure files may be viewed using one of several free and open source computer programs, including Jmol, Pymol, VMD, Rasmol. Other non-free, shareware programs
A hydrogen bond is a electrostatic force of attraction between a hydrogen atom, covalently bound to a more electronegative atom or group the second-row elements nitrogen, oxygen, or fluorine —the hydrogen bond donor —and another electronegative atom bearing a lone pair of electrons—the hydrogen bond acceptor. Such an interacting system is denoted Dn–H···Ac, where the solid line denotes a covalent bond, the dotted line indicates the hydrogen bond. There is general agreement that there is a minor covalent component to hydrogen bonding for moderate to strong hydrogen bonds, although the importance of covalency in hydrogen bonding is debated. At the opposite end of the scale, there is no clear boundary between a weak hydrogen bond and a van der Waals interaction. Weaker hydrogen bonds are known for hydrogen atoms bound to elements such as chlorine; the hydrogen bond is responsible for many of the anomalous physical and chemical properties of compounds of N, O, F. Hydrogen bonds can be intramolecular.
Depending on the nature of the donor and acceptor atoms which constitute the bond, their geometry, environment, the energy of a hydrogen bond can vary between 1 and 40 kcal/mol. This makes them somewhat stronger than a van der Waals interaction, weaker than covalent or ionic bonds; this type of bond can occur in inorganic molecules such as water and in organic molecules like DNA and proteins. Intermolecular hydrogen bonding is responsible for the high boiling point of water compared to the other group 16 hydrides that have much weaker hydrogen bonds. Intramolecular hydrogen bonding is responsible for the secondary and tertiary structures of proteins and nucleic acids, it plays an important role in the structure of polymers, both synthetic and natural. It was recognized that there are many examples of weaker hydrogen bonding involving donor Dn other than N, O, or F and/or acceptor Ac with close to or the same electronegativity as hydrogen. Though they are quite weak, they are ubiquitous and are recognized as important control elements in receptor-ligand interactions in medicinal chemistry or intra-/intermolecular interactions in materials sciences.
Thus, there is a trend of gradual broadening for the definition of hydrogen bonding. In 2011, an IUPAC Task Group recommended a modern evidence-based definition of hydrogen bonding, published in the IUPAC journal Pure and Applied Chemistry; this definition specifies: The hydrogen bond is an attractive interaction between a hydrogen atom from a molecule or a molecular fragment X–H in which X is more electronegative than H, an atom or a group of atoms in the same or a different molecule, in which there is evidence of bond formation. Most introductory textbooks still restrict the definition of hydrogen bond to the "classical" type of hydrogen bond characterized in the opening paragraph. A hydrogen atom attached to a electronegative atom is the hydrogen bond donor. C-H bonds only participate in hydrogen bonding when the carbon atom is bound to electronegative substituents, as is the case in chloroform, CHCl3. In a hydrogen bond, the electronegative atom not covalently attached to the hydrogen is named proton acceptor, whereas the one covalently bound to the hydrogen is named the proton donor.
In the donor molecule, the H center is protic. The donor is a Lewis base. Hydrogen bonds are represented as H · · · Y system. Liquids that display hydrogen bonding are called associated liquids; the hydrogen bond is described as an electrostatic dipole-dipole interaction. However, it has some features of covalent bonding: it is directional and strong, produces interatomic distances shorter than the sum of the van der Waals radii, involves a limited number of interaction partners, which can be interpreted as a type of valence; these covalent features are more substantial when acceptors bind hydrogens from more electronegative donors. Hydrogen bonds can vary in strength from weak to strong. Typical enthalpies in vapor include: F−H···:F, illustrated uniquely by HF2−, bifluoride O−H···:N, illustrated water-ammonia O−H···:O, illustrated water-water, alcohol-alcohol N−H···:N, illustrated by ammonia-ammonia N−H···:O, illustrated water-amide HO−H···:OH+3 The strength of intermolecular hydrogen bonds is most evaluated by measurements of equilibria between molecules containing donor and/or acceptor units, most in solution.
The strength of intramolecular hydrogen bonds can be studied with equilibria between conformers with and without hydrogen bonds. The most important method for the identification of hydrogen bonds in complicated molecules is crystallography, sometimes NMR-spectroscopy. Structural details, in particular distances between donor and acceptor which are smaller than the sum of the van der Waals radii can be taken as indication of the hydrogen bond strength. One scheme gives the following somewhat arbitrary classification: those that are 15 to 40 kcal/mol, 5 to 15 kcal/mol, >0 to 5 kcal/mol are considered strong, moder
A chemical reaction is a process that leads to the chemical transformation of one set of chemical substances to another. Classically, chemical reactions encompass changes that only involve the positions of electrons in the forming and breaking of chemical bonds between atoms, with no change to the nuclei, can be described by a chemical equation. Nuclear chemistry is a sub-discipline of chemistry that involves the chemical reactions of unstable and radioactive elements where both electronic and nuclear changes can occur; the substance involved in a chemical reaction are called reactants or reagents. Chemical reactions are characterized by a chemical change, they yield one or more products, which have properties different from the reactants. Reactions consist of a sequence of individual sub-steps, the so-called elementary reactions, the information on the precise course of action is part of the reaction mechanism. Chemical reactions are described with chemical equations, which symbolically present the starting materials, end products, sometimes intermediate products and reaction conditions.
Chemical reactions happen at a characteristic reaction rate at a given temperature and chemical concentration. Reaction rates increase with increasing temperature because there is more thermal energy available to reach the activation energy necessary for breaking bonds between atoms. Reactions may proceed in the forward or reverse direction until they go to completion or reach equilibrium. Reactions that proceed in the forward direction to approach equilibrium are described as spontaneous, requiring no input of free energy to go forward. Non-spontaneous reactions require input of free energy to go forward. Different chemical reactions are used in combinations during chemical synthesis in order to obtain a desired product. In biochemistry, a consecutive series of chemical reactions form metabolic pathways; these reactions are catalyzed by protein enzymes. Enzymes increase the rates of biochemical reactions, so that metabolic syntheses and decompositions impossible under ordinary conditions can occur at the temperatures and concentrations present within a cell.
The general concept of a chemical reaction has been extended to reactions between entities smaller than atoms, including nuclear reactions, radioactive decays, reactions between elementary particles, as described by quantum field theory. Chemical reactions such as combustion in fire and the reduction of ores to metals were known since antiquity. Initial theories of transformation of materials were developed by Greek philosophers, such as the Four-Element Theory of Empedocles stating that any substance is composed of the four basic elements – fire, water and earth. In the Middle Ages, chemical transformations were studied by Alchemists, they attempted, in particular, to convert lead into gold, for which purpose they used reactions of lead and lead-copper alloys with sulfur. The production of chemical substances that do not occur in nature has long been tried, such as the synthesis of sulfuric and nitric acids attributed to the controversial alchemist Jābir ibn Hayyān; the process involved heating of sulfate and nitrate minerals such as copper sulfate and saltpeter.
In the 17th century, Johann Rudolph Glauber produced hydrochloric acid and sodium sulfate by reacting sulfuric acid and sodium chloride. With the development of the lead chamber process in 1746 and the Leblanc process, allowing large-scale production of sulfuric acid and sodium carbonate chemical reactions became implemented into the industry. Further optimization of sulfuric acid technology resulted in the contact process in the 1880s, the Haber process was developed in 1909–1910 for ammonia synthesis. From the 16th century, researchers including Jan Baptist van Helmont, Robert Boyle, Isaac Newton tried to establish theories of the experimentally observed chemical transformations; the phlogiston theory was proposed in 1667 by Johann Joachim Becher. It postulated the existence of a fire-like element called "phlogiston", contained within combustible bodies and released during combustion; this proved to be false in 1785 by Antoine Lavoisier who found the correct explanation of the combustion as reaction with oxygen from the air.
Joseph Louis Gay-Lussac recognized in 1808 that gases always react in a certain relationship with each other. Based on this idea and the atomic theory of John Dalton, Joseph Proust had developed the law of definite proportions, which resulted in the concepts of stoichiometry and chemical equations. Regarding the organic chemistry, it was long believed that compounds obtained from living organisms were too complex to be obtained synthetically. According to the concept of vitalism, organic matter was endowed with a "vital force" and distinguished from inorganic materials; this separation was ended however by the synthesis of urea from inorganic precursors by Friedrich Wöhler in 1828. Other chemists who brought major contributions to organic chemistry include Alexander William Williamson with his synthesis of ethers and Christopher Kelk Ingold, among many discoveries, established the mechanisms of substitution reactions. Chemical equations are used to graphically illustrate chemical reactions, they consist of chemical or structural formulas of the reactants on the left and those of the products on the right.
They are separated by an arrow which indicates the type of the reaction.