|
Soret Peak
In spectroscopy, a Soret peak or Soret band is an intense peak in the blue wavelength region of the visible spectrum. The peak is named after its discoverer, Jacques-Louis Soret. The term is commonly used in absorption spectroscopy, corresponding to a wavelength of maximum absorption (electromagnetic radiation) ranging around 400 nm in the blue region. Examples The Soret band arises primarily due to an electron dipole movement that allows π-π* transitions; most common in porphyrin compounds. Most analytical studies of porphyrincontaining moiety can be done using ultraviolet–visible spectroscopy and exciting wavelength at the respective Soret band wavelength. For example, the "Soret peak" is used to describe the absorption of vividly-pigmented heme-containing moieties, such as various cytochromes. For example, the cytochromes P450, a diverse class of monooxygenase enzymes, exhibit a Soret peak at 450 nm in their reduced form when saturated with carbon monoxide. This i ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Spectroscopy
Spectroscopy is the field of study that measures and interprets the electromagnetic spectra that result from the interaction between electromagnetic radiation and matter as a function of the wavelength or frequency of the radiation. Matter waves and acoustic waves can also be considered forms of radiative energy, and recently gravitational waves have been associated with a spectral signature in the context of the Laser Interferometer Gravitational-Wave Observatory (LIGO) In simpler terms, spectroscopy is the precise study of color as generalized from visible light to all bands of the electromagnetic spectrum. Historically, spectroscopy originated as the study of the wavelength dependence of the absorption by gas phase matter of visible light dispersed by a prism. Spectroscopy, primarily in the electromagnetic spectrum, is a fundamental exploratory tool in the fields of astronomy, chemistry, materials science, and physics, allowing the composition, physical structure and e ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Moiety (chemistry)
In organic chemistry, a moiety ( ) is a part of a molecule that is given a name because it is identified as a part of other molecules as well. Typically, the term is used to describe the larger and characteristic parts of organic molecules, and it should not be used to describe or name smaller functional groups of atoms that chemically react in similar ways in most molecules that contain them. Occasionally, a moiety may contain smaller moieties and functional groups. A moiety that acts as a branch extending from the backbone of a hydrocarbon molecule is called a substituent or side chain, which typically can be removed from the molecule and substituted with others. Active moiety In pharmacology, an active moiety is the part of a molecule or ion – excluding appended inactive portions – that is responsible for the physiological or pharmacological action of a drug substance. Inactive appended portions of the drug substance may include either the alcohol or acid moiety of ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Taylor & Francis
Taylor & Francis Group is an international company originating in England that publishes books and academic journals. Its parts include Taylor & Francis, Routledge, F1000 (publisher), F1000 Research or Dovepress. It is a division of Informa, Informa plc, a United Kingdom–based publisher and conference company. Overview The company was founded in 1852 when William Francis (chemist), William Francis joined Richard Taylor (editor), Richard Taylor in his publishing business. Taylor had founded his company in 1798. Their subjects covered agriculture, chemistry, education, engineering, geography, law, mathematics, medicine, and social sciences. Francis's son, Richard Taunton Francis (1883–1930), was sole partner in the firm from 1917 to 1930. In 1965, Taylor & Francis launched Wykeham Publications and began book publishing. T&F acquired Hemisphere Publishing in 1988, and the company was renamed Taylor & Francis Group to reflect the growing number of Imprint (trade name), imp ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Carbon Monoxide
Carbon monoxide (chemical formula CO) is a colorless, poisonous, odorless, tasteless, flammable gas that is slightly less dense than air. Carbon monoxide consists of one carbon atom and one oxygen atom connected by a triple bond. It is the simplest molecule of the oxocarbon family. In coordination complexes the carbon monoxide ligand is called carbonyl. It is a key ingredient in many processes in industrial chemistry. The most common source of carbon monoxide is the partial combustion of carbon-containing compounds, when insufficient oxygen or heat is present to produce carbon dioxide. There are also numerous environmental and biological sources that generate and emit a significant amount of carbon monoxide. It is important in the production of many compounds, including drugs, fragrances, and fuels. Upon emission into the atmosphere, carbon monoxide affects several processes that contribute to climate change. Carbon monoxide has important biological roles across phylogenetic ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Enzyme
Enzymes () are proteins that act as biological catalysts by accelerating chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products. Almost all metabolic processes in the cell need enzyme catalysis in order to occur at rates fast enough to sustain life. Metabolic pathways depend upon enzymes to catalyze individual steps. The study of enzymes is called ''enzymology'' and the field of pseudoenzyme analysis recognizes that during evolution, some enzymes have lost the ability to carry out biological catalysis, which is often reflected in their amino acid sequences and unusual 'pseudocatalytic' properties. Enzymes are known to catalyze more than 5,000 biochemical reaction types. Other biocatalysts are catalytic RNA molecules, called ribozymes. Enzymes' specificity comes from their unique three-dimensional structures. Like all catalysts, enzymes increase the reaction ra ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Monooxygenase
Monooxygenases are enzymes that incorporate one hydroxyl group (−OH) into substrates in many metabolic pathways. In this reaction, the two atoms of dioxygen are reduced to one hydroxyl group and one H2O molecule by the concomitant oxidation of NAD(P)H. One important subset of the monooxygenases, the cytochrome P450 omega hydroxylases, is used by cells to metabolize arachidonic acid (i.e. eicosatetraenoic acid) to the cell signaling molecules, 20-hydroxyeicosatetraenoic acid or to reduce or totally inactivate the activate signaling molecules for example by hydroxylating leukotriene B4 to 20-hydroxy-leukotriene B5, 5-hydroxyeicosatetraenoic acid to 5,20-dihydroxyeicosatetraenoic acid, 5-oxo-eicosatetraenoic acid to 5-oxo-20-hydroxyeicosatetraenoic acid, 12-hydroxyeicosatetraenoic acid to 12,20-dihydroxyeicosatetraenoic acid, and epoxyeicosatrienoic acids to 20-hydroxy-epoxyeicosatrienoic acids. Classification They are classified as oxidoreductase enzymes that catalyzes an ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
P450
Cytochromes P450 (CYPs) are a superfamily of enzymes containing heme as a cofactor that functions as monooxygenases. In mammals, these proteins oxidize steroids, fatty acids, and xenobiotics, and are important for the clearance of various compounds, as well as for hormone synthesis and breakdown. In 1963, Estabrook, Cooper, and Rosenthal described the role of CYP as a catalyst in steroid hormone synthesis and drug metabolism. In plants, these proteins are important for the biosynthesis of defensive compounds, fatty acids, and hormones. CYP enzymes have been identified in all kingdoms of life: animals, plants, fungi, protists, bacteria, and archaea, as well as in viruses. However, they are not omnipresent; for example, they have not been found in ''Escherichia coli''. , more than 300,000 distinct CYP proteins are known. CYPs are, in general, the terminal oxidase enzymes in electron transfer chains, broadly categorized as P450-containing systems. The term "P450" is derived fro ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cytochrome
Cytochromes are redox-active proteins containing a heme, with a central Fe atom at its core, as a cofactor. They are involved in electron transport chain and redox catalysis. They are classified according to the type of heme and its mode of binding. Four varieties are recognized by the International Union of Biochemistry and Molecular Biology (IUBMB), cytochromes a, cytochromes b, cytochromes c and cytochrome d. Cytochrome function is linked to the reversible redox change from ferrous (Fe(II)) to the ferric (Fe(III)) oxidation state of the iron found in the heme core. In addition to the classification by the IUBMB into four cytochrome classes, several additional classifications such as cytochrome o and cytochrome P450 can be found in biochemical literature. History Cytochromes were initially described in 1884 by Charles Alexander MacMunn as respiratory pigments (myohematin or histohematin). In the 1920s, Keilin rediscovered these respiratory pigments and named them the c ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Cytochromes
Cytochromes are redox-active proteins containing a heme, with a central Fe atom at its core, as a Cofactor (biochemistry), cofactor. They are involved in electron transport chain and redox catalysis. They are classified according to the type of heme and its Chemical bond, mode of binding. Four varieties are recognized by the International Union of Biochemistry and Molecular Biology (IUBMB), cytochromes a, Cytochrome b, cytochromes b, Cytochrome c family, cytochromes c and cytochrome d. Cytochrome function is linked to the reversible redox change from ferrous (Fe(II)) to the ferric (Fe(III)) oxidation state of the iron found in the heme core. In addition to the classification by the IUBMB into four cytochrome classes, several additional classifications such as Cytochrome c oxidase, cytochrome o and cytochrome P450 can be found in biochemical literature. History Cytochromes were initially described in 1884 by Charles Alexander MacMunn as respiratory pigments (myohematin or histo ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Heme
Heme, or haem (pronounced / hi:m/ ), is a precursor to hemoglobin, which is necessary to bind oxygen in the bloodstream. Heme is biosynthesized in both the bone marrow and the liver. In biochemical terms, heme is a coordination complex "consisting of an iron ion coordinated to a porphyrin acting as a tetradentate ligand, and to one or two axial ligands." The definition is loose, and many depictions omit the axial ligands. Among the metalloporphyrins deployed by metalloproteins as prosthetic groups, heme is one of the most widely used and defines a family of proteins known as hemoproteins. Hemes are most commonly recognized as components of hemoglobin, the red pigment in blood, but are also found in a number of other biologically important hemoproteins such as myoglobin, cytochromes, catalases, heme peroxidase, and endothelial nitric oxide synthase. The word ''haem'' is derived from Greek ''haima'' meaning "blood". Function Hemoproteins have diverse biological functions incl ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Visible Spectrum
The visible spectrum is the portion of the electromagnetic spectrum that is visual perception, visible to the human eye. Electromagnetic radiation in this range of wavelengths is called ''visible light'' or simply light. A typical human eye will respond to wavelengths from about 380 to about 750 nanometers. In terms of frequency, this corresponds to a band in the vicinity of 400–790 Terahertz (unit), terahertz. These boundaries are not sharply defined and may vary per individual. Under optimal conditions these limits of human perception can extend to 310 nm (ultraviolet) and 1100 nm (near infrared). The optical spectrum is sometimes considered to be the same as the visible spectrum, but some authors define the term more broadly, to include the ultraviolet and infrared parts of the electromagnetic spectrum as well. The spectrum does not contain all the colors that the human visual system can distinguish. ''Excitation purity, Unsaturated colors'' such as pink, or ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ultraviolet–visible Spectroscopy
UV spectroscopy or UV–visible spectrophotometry (UV–Vis or UV/Vis) refers to absorption spectroscopy or reflectance spectroscopy in part of the ultraviolet and the full, adjacent visible regions of the electromagnetic spectrum. Being relatively inexpensive and easily implemented, this methodology is widely used in diverse applied and fundamental applications. The only requirement is that the sample absorb in the UV-Vis region, i.e. be a chromophore. Absorption spectroscopy is complementary to fluorescence spectroscopy. Parameters of interest, besides the wavelength of measurement, are absorbance (A) or transmittance (%T) or reflectance (%R), and its change with time. Optical transitions Most molecules and ions absorb energy in the ultraviolet or visible range, i.e., they are chromophores. The absorbed photon excites an electron in the chromophore to higher energy molecular orbitals, giving rise to an excited state. For organic chromophores, four possible types of transitions ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
.jpg "Click for more on -> Taylor & Francis")
_nickel_(II)_chloride_UV-vis.JPG "Click for more on -> Ultraviolet–visible Spectroscopy")