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Photolyase
Photolyases () are DNA repair enzymes that repair damage caused by exposure to ultraviolet light. These enzymes require visible light (from the violet/blue end of the spectrum) both for their own activation and for the actual DNA repair. The DNA repair mechanism involving photolyases is called photoreactivation. They mainly convert pyrimidine dimers into a normal pair of pyrimidine bases. Photo reactivation, the first DNA repair mechanism to be discovered, was described initially by Albert Kelner in 1949 and independently by Renato Dulbecco also in 1949. Function Photolyases bind complementary DNA strands and break certain types of pyrimidine dimers that arise when a pair of thymine or cytosine bases on the same strand of DNA become covalently linked. The bond length of this dimerization is shorter than the bond length of normal B-DNA structure which produces an incorrect template for replication and transcription. The more common covalent linkage involves the formation of ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cryptochrome
Cryptochromes (from the Greek κρυπτός χρώμα, "hidden colour") are a class of flavoproteins found in plants and animals that are sensitive to blue light. They are involved in the circadian rhythms and the sensing of magnetic fields in a number of species. The name ''cryptochrome'' was proposed as a ''portmanteau'' combining the '' chromatic'' nature of the photoreceptor, and the '' cryptogamic'' organisms on which many blue-light studies were carried out. The genes ''CRY1'' and ''CRY2'' encode the proteins CRY1 and CRY2, respectively. Cryptochromes are classified into plant Cry and animal Cry. Animal Cry can be further categorized into insect type (Type I) and mammal-like (Type II). CRY1 is a circadian photoreceptor whereas CRY2 is a clock repressor which represses Clock/Cycle (Bmal1) complex in insects and vertebrates. In plants, blue-light photoreception can be used to cue developmental signals. Besides chlorophylls, cryptochromes are the only proteins known ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Rice
Rice is a cereal grain and in its Domestication, domesticated form is the staple food of over half of the world's population, particularly in Asia and Africa. Rice is the seed of the grass species ''Oryza sativa'' (Asian rice)—or, much less commonly, ''Oryza glaberrima'' (African rice). Asian rice was domesticated in China some 13,500 to 8,200 years ago; African rice was domesticated in Africa about 3,000 years ago. Rice has become commonplace in many cultures worldwide; in 2023, 800 million tons were produced, placing it third after sugarcane and maize. Only some 8% of rice is traded internationally. China, India, and Indonesia are the largest consumers of rice. A substantial amount of the rice produced in developing nations is lost after harvest through factors such as poor transport and storage. Rice yields can be reduced by pests including insects, rodents, and birds, as well as by weeds, and by List of rice diseases, diseases such as rice blast. Traditional rice polyc ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Arabidopsis Thaliana
''Arabidopsis thaliana'', the thale cress, mouse-ear cress or arabidopsis, is a small plant from the mustard family (Brassicaceae), native to Eurasia and Africa. Commonly found along the shoulders of roads and in disturbed land, it is generally considered a weed. A winter annual with a relatively short lifecycle, ''A. thaliana'' is a popular model organism in plant biology and genetics. For a complex multicellular eukaryote, ''A. thaliana'' has a relatively small genome of around 135 Base pair#Length measurements, megabase pairs. It was the first plant to have its genome sequenced, and is an important tool for understanding the molecular biology of many plant traits, including flower development and phototropism, light sensing. Description ''Arabidopsis thaliana'' is an annual plant, annual (rarely biennial plant, biennial) plant, usually growing to 20–25 cm tall. The leaf, leaves form a rosette at the base of the plant, with a few leaves also on the flowering Plant ste ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Halobacterium Halobium
''Halobacterium salinarum'', formerly known as ''Halobacterium cutirubrum'' or ''Halobacterium halobium'', is an extremely halophilic marine obligate aerobic archaeon. Despite its name, this is not a bacterium, but a member of the domain Archaea. It is found in salted fish, hides, hypersaline lakes, and salterns. As these salterns reach the minimum salinity limits for extreme halophiles, their waters become purple or reddish color due to the high densities of halophilic Archaea. ''H. salinarum'' has also been found in high-salt food such as salt pork, marine fish, and sausages. The ability of ''H. salinarum'' to live at such high salt concentrations has led to its classification as an extremophile. Cell morphology and metabolism Halobacteria are single-celled, rod-shaped microorganisms that are among the most ancient forms of life and appeared on Earth billions of years ago. The membrane consists of a single lipid bilayer surrounded by an S-layer. The S-layer is made of a ce ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Archaea
Archaea ( ) is a Domain (biology), domain of organisms. Traditionally, Archaea only included its Prokaryote, prokaryotic members, but this has since been found to be paraphyletic, as eukaryotes are known to have evolved from archaea. Even though the domain Archaea Cladistics, cladistically includes eukaryotes, the term "archaea" (: archaeon , from the Greek "ἀρχαῖον", which means ancient) in English still generally refers specifically to prokaryotic members of Archaea. Archaea were initially Taxonomy (biology), classified as bacteria, receiving the name archaebacteria (, in the Archaebacteria Kingdom (biology), kingdom), but this term has fallen out of use. Archaeal cells have unique properties separating them from Bacteria and Eukaryote, Eukaryota. Archaea are further divided into multiple recognized phylum, phyla. Classification is difficult because most have not been Isolation (microbiology), isolated in a laboratory and have been detected only by their Gene, gene s ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Electron Transfer
Electron transfer (ET) occurs when an electron relocates from an atom, ion, or molecule, to another such chemical entity. ET describes the mechanism by which electrons are transferred in redox reactions. Electrochemical processes are ET reactions. ET reactions are relevant to photosynthesis and respiration and commonly involve transition metal complexes. In organic chemistry ET is a step in some industrial polymerization reactions. It is foundational to photoredox catalysis. Classes of electron transfer Inner-sphere electron transfer In inner-sphere ET, two redox centers are covalently linked during the ET. This bridge can be permanent, in which case the electron transfer event is termed intramolecular electron transfer. More commonly, however, the covalent linkage is transitory, forming just prior to the ET and then disconnecting following the ET event. In such cases, the electron transfer is termed intermolecular electron transfer. A famous example of an inner sphere ET pr ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Deazaflavin
Coenzyme F420 is a family of coenzymes involved in redox reactions in a number of bacteria and archaea. It is derived from coenzyme FO (7,8-didemethyl-8-hydroxy-5-deazariboflavin) and differs by having a oligoglutamyl tail attached via a 2-phospho-L-lactate bridge. F420 is so named because it is a flavin derivative with an absorption maximum at 420 nm. F420 was originally discovered in methanogenic archaea and in Actinomycetota (especially in ''Mycobacterium''). It is now known to be used also by Cyanobacteria and by soil Proteobacteria, Chloroflexi and Firmicutes. Eukaryotes including the fruit fly ''Drosophila melanogaster'' and the algae ''Ostreococcus tauri'' also use Coenzyme FO. F420 is structurally similar to FMN, but catalytically it is similar to NAD and NADP: it has low redox potential and always transfer a hydride. As a result, it is not only a versatile cofactor in biochemical reactions, but also being eyed for potential as an industrial catalyst. Similar to ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Pterin
Pterin is a heterocyclic compound composed of a pteridine ring system, with a " keto group" (a lactam) and an amino group on positions 4 and 2 respectively. It is structurally related to the parent bicyclic heterocycle called pteridine. Pterins, as a group, are compounds related to pterin with additional substituents. Pterin itself is of no biological significance. Pterins were first discovered in the pigments of butterfly wings (hence the origin of their name, from the Greek ''pteron'' (), wing) and perform many roles in coloration in the biological world. Chemistry Pterins exhibit a wide range of tautomerism in water, beyond what is assumed by just keto-enol tautomerism. For the unsubstituted pterin, at least five tautomers are commonly cited. For 6-methylpterin, seven tautomers are theoretically predicted to be important in solution. The pteridine ring system contains four nitrogen atoms, reducing its aromaticity to the point that it can be attacked by nucleophi ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
FADH
In biochemistry, flavin adenine dinucleotide (FAD) is a redox-active coenzyme associated with various proteins, which is involved with several enzymatic reactions in metabolism. A flavoprotein is a protein that contains a flavin group, which may be in the form of FAD or flavin mononucleotide (FMN). Many flavoproteins are known: components of the succinate dehydrogenase complex, α-ketoglutarate dehydrogenase, and a component of the pyruvate dehydrogenase complex. FAD can exist in four redox states, which are the flavin-N(5)-oxide, quinone, semiquinone, and hydroquinone. FAD is converted between these states by accepting or donating electrons. FAD, in its fully oxidized form, or quinone form, accepts two electrons and two protons to become FADH2 (hydroquinone form). The semiquinone (FADH·) can be formed by either reduction of FAD or oxidation of FADH2 by accepting or donating one electron and one proton, respectively. Some proteins, however, generate and maintain a superoxidize ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
DNA Photolyase N-terminal Domain
DNA photolyase, N-terminal is an evolutionary conserved protein domain. This domain binds a light harvesting chromophore that enhanced the spectrum of photolyase or cryptochrome light absorption, i.e. an antenna. It adopts the Rossmann fold. The cofactor may be either the pterin 5,10-Methenyltetrahydrofolate (MTHF, ) in ''folate photolyases'' () or the deazaflavin 8-hydroxy-7,8-didemethyl-5-deazariboflavin (8-HDF, ) in ''deazaflavin photolyases'' (). The 8-HDF ligand usually binds into this domain (next to the C-terminal half), while MHF tends to bind to an outside groove of this domain. A structural signature for 8-HDF binding has been produced, highlighting amino acid residues that determine which antenna a photolyase can use. Experiments on a ''Thermus thermophilus'' protein with this domain () shows that artificial substrates can be alternatively used for a modified absorption spectra. It naturally binds FMN in a pose similar to 8-HDF. In addition, many cryptochromes, esp ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cofactor (biochemistry)
A cofactor is a non-protein chemical compound or metallic ion that is required for an enzyme's role as a catalyst (a catalyst is a substance that increases the rate of a chemical reaction). Cofactors can be considered "helper molecules" that assist in biochemical transformations. The rates at which these happen are characterized in an area of study called enzyme kinetics. Cofactors typically differ from ligands in that they often derive their function by remaining bound. Cofactors can be classified into two types: inorganic ions and complex organic molecules called coenzymes. Coenzymes are mostly derived from vitamins and other organic essential nutrients in small amounts. (Some scientists limit the use of the term "cofactor" for inorganic substances; both types are included here.) Coenzymes are further divided into two types. The first is called a " prosthetic group", which consists of a coenzyme that is tightly (or even covalently and, therefore, permanently) bound to a ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
