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Bilins
Bilins, bilanes or bile pigments are biological pigments formed in many organisms as a metabolic product of certain porphyrins. Bilin (also called bilichrome) was named as a bile pigment of mammals, but can also be found in lower vertebrates, invertebrates, as well as red algae, green plants and cyanobacteria. Bilins can range in color from red, orange, yellow or brown to blue or green. In chemical terms, bilins are linear arrangements of four pyrrole rings ( tetrapyrroles). In human metabolism, bilirubin is a breakdown product of heme. A modified bilane is an intermediate in the biosynthesis and uroporphyrinogen III from porphobilinogen (PBG). Examples of bilins are found in animals (cardinal examples are bilirubin and biliverdin), and phycocyanobilin, the chromophore of the photosynthetic pigment phycocyanin, in algae and plants. In plants, bilins also serve as the photopigments of the photoreceptor protein phytochrome. An example of an invertebrate bilin is microm ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Phytochrome
Phytochromes are a class of photoreceptor in plants, bacteria and fungi used to detect light. They are sensitive to light in the red and far-red region of the visible spectrum and can be classed as either Type I, which are activated by far-red light, or Type II that are activated by red light. Recent advances have suggested that phytochromes also act as temperature sensors, as warmer temperatures enhance their de-activation. All of these factors contribute to the plant's ability to germinate. Phytochromes control many aspects of plant development. They regulate the germination of seeds (photoblasty), the synthesis of chlorophyll, the elongation of seedlings, the size, shape and number and movement of leaves and the timing of flowering in adult plants. Phytochromes are widely expressed across many tissues and developmental stages. Other plant photoreceptors include cryptochromes and phototropins, which respond to blue and ultraviolet-A light and UVR8, which is sensitive to u ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Bilirubin ZZ
Bilirubin (BR) (Latin for "red bile") is a red-orange compound that occurs in the normal catabolism, catabolic pathway that breaks down heme in vertebrates. This catabolism is a necessary process in the body's clearance of waste products that arise from the destruction of aged or abnormal red blood cells. In the first step of bilirubin synthesis, the heme molecule is stripped from the hemoglobin molecule. Heme then passes through various processes of porphyrin catabolism, which varies according to the region of the body in which the breakdown occurs. For example, the molecules excreted in the urine differ from those in the feces. The production of biliverdin from heme is the first major step in the catabolic pathway, after which the enzyme biliverdin reductase performs the second step, producing bilirubin from biliverdin.Boron W, Boulpaep E. Medical Physiology: a cellular and molecular approach, 2005. 984–986. Elsevier Saunders, United States. Ultimately, bilirubin is broken d ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Phycocyanobilin
Phycocyanobilin is a blue phycobilin, i.e., a tetrapyrrole chromophore found in cyanobacteria and in the chloroplasts of red algae, glaucophytes, and some cryptomonads. Phycocyanobilin is present only in the phycobiliproteins allophycocyanin and phycocyanin, of which it is the terminal acceptor of energy. It is covalently linked to these phycobiliproteins by a thioether In organic chemistry, an organic sulfide (British English sulphide) or thioether is an organosulfur functional group with the connectivity as shown on right. Like many other sulfur-containing compounds, volatile sulfides have foul odors. A su ... bond. Phycocyanobilin, PCB, has the ability to bind to human serum albumin, HSA, protein found mainly in the blood of humans. This PCB-HCA complex benefits the structure of HSA, increasing the thermal stability of HSA, as well as increasing its ability to prevent against proteolytic activity of other proteins. References Further reading * Photosynt ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Lipocalin
The lipocalins are a family of proteins which transport small hydrophobic molecules such as steroids, bilins, retinoids, and lipids and most lipocalins are also able to bind to complexed iron (via siderophores or flavonoids) as well as heme. They share limited regions of sequence homology and a common tertiary structure architecture. This is an eight stranded antiparallel beta barrel with a repeated + 1 topology enclosing an internal ligand binding site. These proteins are found in gram negative bacteria, vertebrate cells, and invertebrate cells, and in plants. Lipocalins have been associated with many biological processes, among them immune response, pheromone transport, biological prostaglandin synthesis, retinoid binding, and cancer cell interactions. Function Immune response Lipocalin proteins are important key players of nutritional immunity by withholding and sequestering micronutrients. They are thereby able to regulate inflammatory and detoxification processe ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Retrograde Signaling
Retrograde signaling in biology is the process where a signal travels backwards from a target source to its original source. For example, the nucleus of a cell is the original source for creating signaling proteins. During retrograde signaling, instead of signals leaving the nucleus, they are sent to the nucleus. In cell biology, this type of signaling typically occurs between the mitochondria or chloroplast and the nucleus. Signaling molecules from the mitochondria or chloroplast act on the nucleus to affect nuclear gene expression. In this regard, the chloroplast or mitochondria act as a sensor for internal external stimuli which activate a signaling pathway. In neuroscience, retrograde signaling (or retrograde neurotransmission) refers more specifically to the process by which a retrograde messenger, such as anandamide or nitric oxide, is released by a postsynaptic dendrite or cell body, and travels "backwards" across a chemical synapse to bind to the axon terminal of a pre ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Chlamydomonas Reinhardtii
''Chlamydomonas reinhardtii'' is a single-cell green alga about 10 micrometres in diameter that swims with two flagella. It has a cell wall made of hydroxyproline-rich glycoproteins, a large cup-shaped chloroplast, a large pyrenoid, and an eyespot that senses light. '' Chlamydomonas'' species are widely distributed worldwide in soil and fresh water. ''Chlamydomonas reinhardtii'' is an especially well studied biological model organism, partly due to its ease of culturing and the ability to manipulate its genetics. When illuminated, ''C. reinhardtii'' can grow photoautotrophically, but it can also grow in the dark if supplied with organic carbon. Commercially, ''C. reinhardtii'' is of interest for producing biopharmaceuticals and biofuel, as well being a valuable research tool in making hydrogen. History The ''C. reinhardtii'' wild-type laboratory strain c137 (mt+) originates from an isolate collected near Amherst, Massachusetts, in 1945 by Gilbert M. Smith. The species' n ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protoporphyrin IX
Protoporphyrin IX is an organic compound, classified as a porphyrin, that plays an important role in living organisms as a precursor to other critical compounds like heme (hemoglobin) and chlorophyll. It is a deeply colored solid that is not soluble in water. The name is often abbreviated as PPIX. Protoporphyrin IX contains a porphine core, a tetrapyrrole macrocycle with a marked aromatic character. Protoporphyrin IX is essentially planar, except for the N-H bonds that are bent out of the plane of the rings, in opposite (trans) directions. Nomenclature The general term protoporphyrin refers to porphine derivatives that have the outer hydrogen atoms in the four pyrrole rings replaced by other functional groups. The prefix proto often means 'first' in science nomenclature (such as carbon protoxide), hence Hans Fischer is thought to have coined the name protoporphyrin as the first class of porphyrins. Fischer described iron-deprived heme becoming the "proto-" porphyrin, particu ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Mg²⁺
Magnesium is a chemical element with the symbol Mg and atomic number 12. It is a shiny gray metal having a low density, low melting point and high chemical reactivity. Like the other alkaline earth metals (group 2 of the periodic table) it occurs naturally only in combination with other elements and it almost always has an oxidation state of +2. It reacts readily with air to form a thin passivation coating of magnesium oxide that inhibits further corrosion of the metal. The free metal burns with a brilliant-white light. The metal is obtained mainly by electrolysis of magnesium salts obtained from brine. It is less dense than aluminium and is used primarily as a component in strong and lightweight alloys that contain aluminium. In the cosmos, magnesium is produced in large, aging stars by the sequential addition of three helium nuclei to a carbon nucleus. When such stars explode as supernovas, much of the magnesium is expelled into the interstellar medium where it ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Magnesium Chelatase
Magnesium-chelatase is a three-component enzyme () that catalyses the insertion of Mg2+ into protoporphyrin IX. This is the first unique step in the synthesis of chlorophyll and bacteriochlorophyll. As a result, it is thought that Mg-chelatase has an important role in channeling intermediates into the (bacterio)chlorophyll branch in response to conditions suitable for photosynthetic growth: protoporphyrin IX + + ATP + \rightleftharpoons ADP + phosphate + Mg-protoporphyrin IX + 2 The four substrates of this enzyme are ATP, protoporphyrin IX, Mg2+, and H2O; its four products are ADP, phosphate, Mg-protoporphyrin IX, and H+. This enzyme belongs to the family of ligases, specifically those forming nitrogen-D-metal bonds in coordination complexes. The systematic name of this enzyme class is Mg-protoporphyrin IX magnesium-lyase. Other names in common use include protoporphyrin IX magnesium-chelatase, protoporphyrin IX Mg-chelatase, magnesium-protoporphyrin IX chelatase, ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Micrommata Virescens
''Micrommata virescens'', common name green huntsman spider, is a species of huntsman spiders belonging to the family Sparassidae. Distribution This species has a Palearctic realm, Palearctic distribution. It occurs naturally in Northern and Central Europe, including Denmark and southern Britain. Description In the females of ''Micrommata virescens'' the body length can reach , while in the males it is about . The cephalothorax and the long legs of the females are bright green, with a lighter green abdomen showing a darker green median stripe. The eight eyes are arranged in two rows and surrounded by white hairs. Males are dark green-olive and have a narrower abdomen, with red sides and a red to red-brown median stripe bordered yellow. (see section 'Thursday, 22 October 2015, Sparassidae: huntsman spiders') ''abugblog.blogspot.it'', accessed 7 August 2022 [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Micromatabilin
Micromatabilin, the green pigment of the spider species ''Micrommata virescens'', is characterized as a mixture of biliverdin Biliverdin (latin for green bile) is a green tetrapyrrolic bile pigment, and is a product of heme catabolism.Boron W, Boulpaep E. Medical Physiology: a cellular and molecular approach, 2005. 984-986. Elsevier Saunders, United States. It is the ... conjugates. The two isolated fractions have identical absorption bands (free base: 620–630 μm, hydrochloride: 690 μm, zinc complex: 685–690 μm). Chromic acid degradation yields imides I, II, IIIa, and IIIb. Differences in the non-hydrolytic degradation and in polarity lead to the conclusion that fraction 1 is a monoconjugate and fraction 2a diconjugate of biliverdin. References Biological pigments Tetrapyrroles {{biochem-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Photoreceptor Protein
Photoreceptor proteins are light-sensitive proteins involved in the sensing and response to light in a variety of organisms. Some examples are rhodopsin in the photoreceptor cells of the vertebrate retina, phytochrome in plants, and bacteriorhodopsin and bacteriophytochromes in some bacteria. They mediate light responses as varied as visual perception, phototropism and phototaxis, as well as responses to light-dark cycles such as circadian rhythm and other photoperiodisms including control of flowering times in plants and mating seasons in animals. Structure Photoreceptor proteins typically consist of a protein attached to a non-protein chromophore (sometimes referred as photopigment, even so photopigment may also refer to the photoreceptor as a whole). The chromophore reacts to light via photoisomerization or photoreduction, thus initiating a change of the receptor protein which triggers a signal transduction cascade. Chromophores found in photoreceptors include retinal (reti ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
