Sulfur dioxideSulfur dioxide (IUPAC-recommended spelling) or sulphur dioxide (traditional Commonwealth English) is the chemical compound with the formula SO2. It is a toxic gas responsible for the odor of burnt matches. It is released naturally by volcanic activity and is produced as a by-product of copper extraction and the burning of sulfur-bearing fossil fuels. SO2 is a bent molecule with C2v symmetry point group. A valence bond theory approach considering just s and p orbitals would describe the bonding in terms of resonance between two resonance structures.
Sulfur metabolismSulfur is metabolized by all organisms, from bacteria and archaea to plants and animals. Sulfur can have an oxidation state from -2 to +6 and is reduced or oxidized by a diverse range of organisms. The element is present in proteins, sulfate esters of polysaccharides, steroids, phenols, and sulfur-containing coenzymes. Reduced sulfur compounds are oxidized by most organisms, including higher animals and higher plants. Some organisms can conserve energy (i.e.
Green sulfur bacteriaThe green sulfur bacteria, Chlorobiota, are a phylum of obligately anaerobic photoautotrophic bacteria that metabolize sulfur. Green sulfur bacteria are nonmotile (except Chloroherpeton thalassium, which may glide) and capable of anoxygenic photosynthesis. They live in anaerobic aquatic environments. In contrast to plants, green sulfur bacteria mainly use sulfide ions as electron donors. They are autotrophs that utilize the reverse tricarboxylic acid cycle to perform carbon fixation. They are also mixotrophs and reduce nitrogen.
Peripheral membrane proteinPeripheral membrane proteins, or extrinsic membrane proteins, are membrane proteins that adhere only temporarily to the biological membrane with which they are associated. These proteins attach to integral membrane proteins, or penetrate the peripheral regions of the lipid bilayer. The regulatory protein subunits of many ion channels and transmembrane receptors, for example, may be defined as peripheral membrane proteins.
Purple sulfur bacteriaThe purple sulfur bacteria (PSB) are part of a group of Pseudomonadota capable of photosynthesis, collectively referred to as purple bacteria. They are anaerobic or microaerophilic, and are often found in stratified water environments including hot springs, stagnant water bodies, as well as microbial mats in intertidal zones. Unlike plants, algae, and cyanobacteria, purple sulfur bacteria do not use water as their reducing agent, and therefore do not produce oxygen.
CysteineCysteine (symbol Cys or C; ˈsɪstɪiːn) is a semiessential proteinogenic amino acid with the formula . The thiol side chain in cysteine often participates in enzymatic reactions as a nucleophile. Cysteine is chiral, only L-cysteine is found in nature. The thiol is susceptible to oxidation to give the disulfide derivative cystine, which serves an important structural role in many proteins. In this case, the symbol Cyx is sometimes used. The deprotonated form can generally be described by the symbol Cym as well.
Cytoplasmic streamingCytoplasmic streaming, also called protoplasmic streaming and cyclosis, is the flow of the cytoplasm inside the cell, driven by forces from the cytoskeleton. It is likely that its function is, at least in part, to speed up the transport of molecules and organelles around the cell. It is usually observed in large plant and animal cells, greater than approximately 0.1 mm. In smaller cells, the diffusion of molecules is more rapid, but diffusion slows as the size of the cell increases, so larger cells may need cytoplasmic streaming for efficient function.
Cysteine proteaseCysteine proteases, also known as thiol proteases, are hydrolase enzymes that degrade proteins. These proteases share a common catalytic mechanism that involves a nucleophilic cysteine thiol in a catalytic triad or dyad. Discovered by Gopal Chunder Roy in 1873, the first cysteine protease to be isolated and characterized was papain, obtained from Carica papaya. Cysteine proteases are commonly encountered in fruits including the papaya, pineapple, fig and kiwifruit. The proportion of protease tends to be higher when the fruit is unripe.
Expressed sequence tagIn genetics, an expressed sequence tag (EST) is a short sub-sequence of a cDNA sequence. ESTs may be used to identify gene transcripts, and were instrumental in gene discovery and in gene-sequence determination. The identification of ESTs has proceeded rapidly, with approximately 74.2 million ESTs now available in public databases (e.g. GenBank 1 January 2013, all species). EST approaches have largely been superseded by whole genome and transcriptome sequencing and metagenome sequencing.
Catalytic triadA catalytic triad is a set of three coordinated amino acids that can be found in the active site of some enzymes. Catalytic triads are most commonly found in hydrolase and transferase enzymes (e.g. proteases, amidases, esterases, acylases, lipases and β-lactamases). An acid-base-nucleophile triad is a common motif for generating a nucleophilic residue for covalent catalysis. The residues form a charge-relay network to polarise and activate the nucleophile, which attacks the substrate, forming a covalent intermediate which is then hydrolysed to release the product and regenerate free enzyme.
Protein productionProtein production is the biotechnological process of generating a specific protein. It is typically achieved by the manipulation of gene expression in an organism such that it expresses large amounts of a recombinant gene. This includes the transcription of the recombinant DNA to messenger RNA (mRNA), the translation of mRNA into polypeptide chains, which are ultimately folded into functional proteins and may be targeted to specific subcellular or extracellular locations.
Homology (biology)In biology, homology is similarity due to shared ancestry between a pair of structures or genes in different taxa. A common example of homologous structures is the forelimbs of vertebrates, where the wings of bats and birds, the arms of primates, the front flippers of whales and the forelegs of four-legged vertebrates like dogs and crocodiles are all derived from the same ancestral tetrapod structure. Evolutionary biology explains homologous structures adapted to different purposes as the result of descent with modification from a common ancestor.
