Electron transport chainAn electron transport chain (ETC) is a series of protein complexes and other molecules that 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. The electrons that are transferred from NADH and FADH2 to the ETC involves four multi-subunit large enzymes complexes and two mobile electron carriers.
Electron donorIn chemistry, an electron donor is a chemical entity that donates electrons to another compound. It is a reducing agent that, by virtue of its donating electrons, is itself oxidized in the process. Typical reducing agents undergo permanent chemical alteration through covalent or ionic reaction chemistry. This results in the complete and irreversible transfer of one or more electrons. In many chemical circumstances, however, the transfer of electronic charge to an electron acceptor may be only fractional, meaning an electron is not completely transferred, but results in an electron resonance between the donor and acceptor.
Sulfate-reducing microorganismSulfate-reducing microorganisms (SRM) or sulfate-reducing prokaryotes (SRP) are a group composed of sulfate-reducing bacteria (SRB) and sulfate-reducing archaea (SRA), both of which can perform anaerobic respiration utilizing sulfate (SO42-) as terminal electron acceptor, reducing it to hydrogen sulfide (H2S). Therefore, these sulfidogenic microorganisms "breathe" sulfate rather than molecular oxygen (O2), which is the terminal electron acceptor reduced to water (H2O) in aerobic respiration.
Doping (semiconductor)In semiconductor production, doping is the intentional introduction of impurities into an intrinsic semiconductor for the purpose of modulating its electrical, optical and structural properties. The doped material is referred to as an extrinsic semiconductor. Small numbers of dopant atoms can change the ability of a semiconductor to conduct electricity. When on the order of one dopant atom is added per 100 million atoms, the doping is said to be low or light.
Sulfur-reducing bacteriaSulfur-reducing bacteria are microorganisms able to reduce elemental sulfur (S0) to hydrogen sulfide (H2S). These microbes use inorganic sulfur compounds as electron acceptors to sustain several activities such as respiration, conserving energy and growth, in absence of oxygen. The final product of these processes, sulfide, has a considerable influence on the chemistry of the environment and, in addition, is used as electron donor for a large variety of microbial metabolisms.
G proteinG proteins, also known as guanine nucleotide-binding proteins, are a family of proteins that act as molecular switches inside cells, and are involved in transmitting signals from a variety of stimuli outside a cell to its interior. Their activity is regulated by factors that control their ability to bind to and hydrolyze guanosine triphosphate (GTP) to guanosine diphosphate (GDP). When they are bound to GTP, they are 'on', and, when they are bound to GDP, they are 'off'. G proteins belong to the larger group of enzymes called GTPases.
Anaerobic organismAn anaerobic organism or anaerobe is any organism that does not require molecular oxygen for growth. It may react negatively or even die if free oxygen is present. In contrast, an aerobic organism (aerobe) is an organism that requires an oxygenated environment. Anaerobes may be unicellular (e.g. protozoans, bacteria) or multicellular. Most fungi are obligate aerobes, requiring oxygen to survive. However, some species, such as the Chytridiomycota that reside in the rumen of cattle, are obligate anaerobes; for these species, anaerobic respiration is used because oxygen will disrupt their metabolism or kill them.
Oxidative phosphorylationOxidative phosphorylation (UK ɒkˈsɪd.ə.tɪv, US ˈɑːk.sɪˌdeɪ.tɪv ) or electron transport-linked phosphorylation or terminal oxidation is the metabolic pathway in which cells use enzymes to oxidize nutrients, thereby releasing chemical energy in order to produce adenosine triphosphate (ATP). In eukaryotes, this takes place inside mitochondria. Almost all aerobic organisms carry out oxidative phosphorylation. This pathway is so pervasive because it releases more energy than alternative fermentation processes such as anaerobic glycolysis.
Anaerobic respirationAnaerobic respiration is respiration using electron acceptors other than molecular oxygen (O2). Although oxygen is not the final electron acceptor, the process still uses a respiratory electron transport chain. In aerobic organisms undergoing respiration, electrons are shuttled to an electron transport chain, and the final electron acceptor is oxygen. Molecular oxygen is an excellent electron acceptor. Anaerobes instead use less-oxidizing substances such as nitrate (NO3-), fumarate (C4H2O42-), sulfate (SO42-), or elemental sulfur (S).
Nicotinamide adenine dinucleotideNicotinamide adenine dinucleotide (NAD) is a coenzyme central to metabolism. Found in all living cells, NAD is called a dinucleotide because it consists of two nucleotides joined through their phosphate groups. One nucleotide contains an adenine nucleobase and the other, nicotinamide. NAD exists in two forms: an oxidized and reduced form, abbreviated as NAD and NADH (H for hydrogen), respectively.
Electron acceptorAn electron acceptor is a chemical entity that accepts electrons transferred to it from another compound. It is an oxidizing agent that, by virtue of its accepting electrons, is itself reduced in the process. Electron acceptors are sometimes mistakenly called electron receptors. The electron accepting power of an acceptor molecule is measured by its electron affinity (A) which is the energy released when filling the lowest unoccupied molecular orbital (LUMO).
Electron affinityThe electron affinity (Eea) of an atom or molecule is defined as the amount of energy released when an electron attaches to a neutral atom or molecule in the gaseous state to form an anion. X(g) + e− → X−(g) + energy This differs by sign from the energy change of electron capture ionization. The electron affinity is positive when energy is released on electron capture. In solid state physics, the electron affinity for a surface is defined somewhat differently (see below).
ProteomicsProteomics is the large-scale study of proteins. Proteins are vital parts of living organisms, with many functions such as the formation of structural fibers of muscle tissue, enzymatic digestion of food, or synthesis and replication of DNA. In addition, other kinds of proteins include antibodies that protect an organism from infection, and hormones that send important signals throughout the body. The proteome is the entire set of proteins produced or modified by an organism or system.
Protein foldingProtein folding is the physical process where a protein chain is translated into its native three-dimensional structure, typically a "folded" conformation, by which the protein becomes biologically functional. Via an expeditious and reproducible process, a polypeptide folds into its characteristic three-dimensional structure from a random coil. Each protein exists first as an unfolded polypeptide or random coil after being translated from a sequence of mRNA into a linear chain of amino acids.
Proton pumpA proton pump is an integral membrane protein pump that builds up a proton gradient across a biological membrane. Proton pumps catalyze the following reaction: H+[on one side of a biological membrane] + energy H+[on the other side of the membrane] 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.
ChemiosmosisChemiosmosis is the movement of ions across a semipermeable membrane bound structure, down their electrochemical gradient. An important example is the formation of adenosine triphosphate (ATP) by the movement of hydrogen ions (H+) across a membrane during cellular respiration or photosynthesis. Hydrogen ions, or protons, will diffuse from a region of high proton concentration to a region of lower proton concentration, and an electrochemical concentration gradient of protons across a membrane can be harnessed to make ATP.
Electron mobilityIn solid-state physics, the electron mobility characterises how quickly an electron can move through a metal or semiconductor when pulled by an electric field. There is an analogous quantity for holes, called hole mobility. The term carrier mobility refers in general to both electron and hole mobility. Electron and hole mobility are special cases of electrical mobility of charged particles in a fluid under an applied electric field. When an electric field E is applied across a piece of material, the electrons respond by moving with an average velocity called the drift velocity, .
PhosphorylationIn biochemistry, phosphorylation is the attachment of a phosphate group to a molecule or an ion. This process and its inverse, dephosphorylation, are common in biology. Protein phosphorylation often activates (or deactivates) many enzymes. Phosphorylation is essential to the processes of both anaerobic and aerobic respiration, which involve the production of adenosine triphosphate (ATP), the "high-energy" exchange medium in the cell.
Inner sphere electron transferInner sphere electron transfer (IS ET) or bonded electron transfer is a redox chemical reaction that proceeds via a covalent linkage—a strong electronic interaction—between the oxidant and the reductant reactants. In inner sphere electron transfer, a ligand bridges the two metal redox centers during the electron transfer event. Inner sphere reactions are inhibited by large ligands, which prevent the formation of the crucial bridged intermediate. Thus, inner sphere ET is rare in biological systems, where redox sites are often shielded by bulky proteins.
Gq alpha subunitDISPLAYTITLE:Gq alpha subunit Gq protein alpha subunit is a family of heterotrimeric G protein alpha subunits. This family is also commonly called the Gq/11 (Gq/G11) family or Gq/11/14/15 family to include closely related family members. G alpha subunits may be referred to as Gq alpha, Gαq, or Gqα. Gq proteins couple to G protein-coupled receptors to activate beta-type phospholipase C (PLC-β) enzymes. PLC-β in turn hydrolyzes phosphatidylinositol 4,5-bisphosphate (PIP2) to diacyl glycerol (DAG) and inositol trisphosphate (IP3).
