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Formate Dehydrogenase
Formate dehydrogenases are a set of enzymes that catalyse the oxidation of formate to carbon dioxide, donating the electrons to a second substrate, such as NAD+ in formate:NAD+ oxidoreductase () or to a cytochrome in formate:ferricytochrome-b1 oxidoreductase (). This family of enzymes has attracted attention as inspiration or guidance on methods for the carbon dioxide fixation, relevant to global warming. Function NAD-dependent formate dehydrogenases are important in methylotrophic yeast and bacteria, being vital in the catabolism of C1 compounds such as methanol. The cytochrome-dependent enzymes are more important in anaerobic metabolism in prokaryotes. For example, in '' E. coli'', the formate:ferricytochrome-b1 oxidoreductase is an intrinsic membrane protein with two subunits and is involved in anaerobic nitrate respiration. NAD-dependent reaction Formate + NAD+ CO2 + NADH + H+ Cytochrome-dependent reaction Formate + 2 ferricytochrome b1 CO2 + 2 ferrocytochrome b1 + ... [...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] |
Formate
Formate (IUPAC name: methanoate) is the conjugate base of formic acid. Formate is an anion () or its derivatives such as ester of formic acid. The salts and esters are generally colorless.Werner Reutemann and Heinz Kieczka "Formic Acid" in ''Ullmann's Encyclopedia of Industrial Chemistry'' 2002, Wiley-VCH, Weinheim. Fundamentals When dissolved in water, formic acid converts to formate: : Formate is a planar anion. The two oxygen atoms are equivalent and bear a partial negative charge. The remaining C-H bond is not acidic. Biochemistry : Formate is a common C-1 source in living systems. It is formed from many precursors including choline, serine, and sarcosine. It provides a C-1 source in the biosynthesis of some nucleic acids. Formate (or formic acid) is ina leaving group in the demethylation of some sterols.. These conversions are catalyzed by aromatase enzymes using O2 as the oxidant. Specific conversions include testosterone to estradiol and androstenedione to estrone ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Carbon Dioxide
Carbon dioxide (chemical formula ) is a chemical compound made up of molecules that each have one carbon atom covalently double bonded to two oxygen atoms. It is found in the gas state at room temperature. In the air, carbon dioxide is transparent to visible light but absorbs infrared radiation, acting as a greenhouse gas. It is a trace gas in Earth's atmosphere at 421 parts per million (ppm), or about 0.04% by volume (as of May 2022), having risen from pre-industrial levels of 280 ppm. Burning fossil fuels is the primary cause of these increased CO2 concentrations and also the primary cause of climate change.IPCC (2022Summary for policy makersiClimate Change 2022: Mitigation of Climate Change. Contribution of Working Group III to the Sixth Assessment Report of the Intergovernmental Panel on Climate Change Cambridge University Press, Cambridge, United Kingdom and New York, NY, USA Carbon dioxide is soluble in water and is found in groundwater, lakes, ice caps, ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nicotinamide Adenine Dinucleotide
Nicotinamide 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. In metabolism, nicotinamide adenine dinucleotide is involved in redox reactions, carrying electrons from one reaction to another. The cofactor is, therefore, found in two forms in cells: NAD is an oxidizing agent – it accepts electrons from other molecules and becomes reduced. This reaction, also with H+, forms NADH, which can then be used as a reducing agent to donate electrons. These electron transfer reactions are the main function of NAD. However, it is also used in other cellular processes, most notably as a substrate of enzymes in adding or removing chemical groups to ... [...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] |
Global Warming
In common usage, climate change describes global warming—the ongoing increase in global average temperature—and its effects on Earth's climate system. Climate change in a broader sense also includes previous long-term changes to Earth's climate. The current rise in global average temperature is more rapid than previous changes, and is primarily caused by humans burning fossil fuels. Fossil fuel use, deforestation, and some agricultural and industrial practices increase greenhouse gases, notably carbon dioxide and methane. Greenhouse gases absorb some of the heat that the Earth radiates after it warms from sunlight. Larger amounts of these gases trap more heat in Earth's lower atmosphere, causing global warming. Due to climate change, deserts are expanding, while heat waves and wildfires are becoming more common. Increased warming in the Arctic has contributed to melting permafrost, glacial retreat and sea ice loss. Higher temperatures are also causing m ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Methylotroph
Methylotrophs are a diverse group of microorganisms that can use reduced one-carbon compounds, such as methanol or methane, as the carbon source for their growth; and multi-carbon compounds that contain no carbon-carbon bonds, such as dimethyl ether and dimethylamine. This group of microorganisms also includes those capable of assimilating reduced one-carbon compounds by way of carbon dioxide using the ribulose bisphosphate pathway. These organisms should not be confused with methanogens which on the contrary produce methane as a by-product from various one-carbon compounds such as carbon dioxide. Some methylotrophs can degrade the greenhouse gas methane, and in this case they are called methanotrophs. The abundance, purity, and low price of methanol compared to commonly used sugars make methylotrophs competent organisms for production of amino acids, vitamins, recombinant proteins, single-cell proteins, co-enzymes and cytochromes. Metabolism The key intermediate in methylotr ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Yeast
Yeasts are eukaryotic, single-celled microorganisms classified as members of the fungus kingdom. The first yeast originated hundreds of millions of years ago, and at least 1,500 species are currently recognized. They are estimated to constitute 1% of all described fungal species. Yeasts are unicellular organisms that evolved from multicellular ancestors, with some species having the ability to develop multicellular characteristics by forming strings of connected budding cells known as pseudohyphae or false hyphae. Yeast sizes vary greatly, depending on species and environment, typically measuring 3–4 µm in diameter, although some yeasts can grow to 40 µm in size. Most yeasts reproduce asexually by mitosis, and many do so by the asymmetric division process known as budding. With their single-celled growth habit, yeasts can be contrasted with molds, which grow hyphae. Fungal species that can take both forms (depending on temperature or other conditions) are ca ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Bacteria
Bacteria (; singular: bacterium) are ubiquitous, mostly free-living organisms often consisting of one biological cell. They constitute a large domain of prokaryotic microorganisms. Typically a few micrometres in length, bacteria were among the first life forms to appear on Earth, and are present in most of its habitats. Bacteria inhabit soil, water, acidic hot springs, radioactive waste, and the deep biosphere of Earth's crust. Bacteria are vital in many stages of the nutrient cycle by recycling nutrients such as the fixation of nitrogen from the atmosphere. The nutrient cycle includes the decomposition of dead bodies; bacteria are responsible for the putrefaction stage in this process. In the biological communities surrounding hydrothermal vents and cold seeps, extremophile bacteria provide the nutrients needed to sustain life by converting dissolved compounds, such as hydrogen sulphide and methane, to energy. Bacteria also live in symbiotic and parasitic relationsh ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Methanol
Methanol (also called methyl alcohol and wood spirit, amongst other names) is an organic chemical and the simplest aliphatic alcohol, with the formula C H3 O H (a methyl group linked to a hydroxyl group, often abbreviated as MeOH). It is a light, volatile, colourless, flammable liquid with a distinctive alcoholic odour similar to that of ethanol (potable alcohol). A polar solvent, methanol acquired the name wood alcohol because it was once produced chiefly by the destructive distillation of wood. Today, methanol is mainly produced industrially by hydrogenation of carbon monoxide. Methanol consists of a methyl group linked to a polar hydroxyl group. With more than 20 million tons produced annually, it is used as a precursor to other commodity chemicals, including formaldehyde, acetic acid, methyl tert-butyl ether, methyl benzoate, anisole, peroxyacids, as well as a host of more specialised chemicals. Occurrence Small amounts of methanol are present in normal, healthy hu ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
DMSO Reductase
DMSO reductase is a molybdenum-containing enzyme that catalyzes reduction of dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS). This enzyme serves as the terminal reductase under anaerobic conditions in some bacteria, with DMSO being the terminal electron acceptor. During the course of the reaction, the oxygen atom in DMSO is transferred to molybdenum, and then reduced to water. DMSO reductase (DMSOR) and other members of the DMSO reductase family are unique to bacteria and archaea. Enzymes of this family in anaerobic oxidative phosphorylation and inorganic-donor-based lithotrophic respiration. These enzymes have been engineered to degrade oxoanions. DMSOR catalyzes the transfer of two electrons and one oxygen atom in the reaction: The active site of DMSOR contains molybdenum, which is otherwise rare in biology. Tertiary structure and active site As for other members of DMSO reductase family, the tertiary structure of DMSOR is composed of Mo-surrounding domains I-I ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Molybdopterin
Molybdopterins are a class of cofactors found in most molybdenum-containing and all tungsten-containing enzymes. Synonyms for molybdopterin are: MPT and pyranopterin-dithiolate. The nomenclature for this biomolecule can be confusing: Molybdopterin itself contains no molybdenum; rather, this is the name of the ligand (a ''pterin'') that will bind the active metal. After molybdopterin is eventually complexed with molybdenum, the complete ligand is usually called molybdenum cofactor. Molybdopterin consists of a pyranopterin, a complex heterocycle featuring a pyran fused to a pterin ring. In addition, the pyran ring features two thiolates, which serve as ligands in molybdo- and tungstoenzymes. In some cases, the alkyl phosphate group is replaced by an alkyl diphosphate nucleotide. Enzymes that contain the molybdopterin cofactor include xanthine oxidase, DMSO reductase, sulfite oxidase, and nitrate reductase. The only molybdenum-containing enzymes that do not feature molybdopteri ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
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