Formate Dehydrogenase (NADP )
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Formate Dehydrogenase (NADP )
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 Nicotinamide adenine dinucleotide, 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 b ...
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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 ...
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Formate Dehydrogenase H
Formate dehydrogenase (acceptor) (, ''FDHH'', ''FDH-H'', ''FDH-O'', ''formate dehydrogenase H'', ''formate dehydrogenase O'') is an enzyme with systematic name ''formate:acceptor oxidoreductase''. This enzyme catalyses the following chemical reaction : formate + acceptor \rightleftharpoons CO2 + reduced acceptor Formate dehydrogenase H is a cytoplasmic enzyme that oxidizes 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 ''Ull ... without oxygen transfer] transferring electrons to a hydrogenase. References External links * {{Portal bar, Biology, border=no EC 1.1.99 ...
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Metabolism
Metabolism (, from el, μεταβολή ''metabolē'', "change") is the set of life-sustaining chemical reactions in organisms. The three main functions of metabolism are: the conversion of the energy in food to energy available to run cellular processes; the conversion of food to building blocks for proteins, lipids, nucleic acids, and some carbohydrates; and the elimination of metabolic wastes. These enzyme-catalyzed reactions allow organisms to grow and reproduce, maintain their structures, and respond to their environments. The word metabolism can also refer to the sum of all chemical reactions that occur in living organisms, including digestion and the transportation of substances into and between different cells, in which case the above described set of reactions within the cells is called intermediary (or intermediate) metabolism. Metabolic reactions may be categorized as ''catabolic'' – the ''breaking down'' of compounds (for example, of glucose to pyruvate by ce ...
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Cellular Respiration
Cellular respiration is the process by which biological fuels are oxidised in the presence of an inorganic electron acceptor such as oxygen to produce large amounts of energy, to drive the bulk production of ATP. Cellular respiration may be described as a set of metabolic reactions and processes that take place in the cells of organisms to convert chemical energy from nutrients into adenosine triphosphate (ATP), and then release waste products. The reactions involved in respiration are catabolic reactions, which break large molecules into smaller ones, releasing energy. Respiration is one of the key ways a cell releases chemical energy to fuel cellular activity. The overall reaction occurs in a series of biochemical steps, some of which are redox reactions. Although cellular respiration is technically a combustion reaction, it is an unusual one because of the slow, controlled release of energy from the series of reactions. Nutrients that are commonly used by animal and plan ...
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Microbial Metabolism
Microbial metabolism is the means by which a microbe obtains the energy and nutrients (e.g. carbon) it needs to live and reproduce. Microbes use many different types of metabolic strategies and species can often be differentiated from each other based on metabolic characteristics. The specific metabolic properties of a microbe are the major factors in determining that microbe's ecological niche, and often allow for that microbe to be useful in industrial processes or responsible for biogeochemical cycles. Types All microbial metabolisms can be arranged according to three principles: 1. How the organism obtains carbon for synthesizing cell mass:Morris, J. et al. (2019). "Biology: How Life Works", 3rd edition, W. H. Freeman. * autotrophic – carbon is obtained from carbon dioxide () * heterotrophic – carbon is obtained from organic compounds * mixotrophic – carbon is obtained from both organic compounds and by fixing carbon dioxide 2. How the organism obtains reducing e ...
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Formate Dehydrogenase (NADP+)
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 Nicotinamide adenine dinucleotide, 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 b ...
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Formate Dehydrogenase (cytochrome-c-553)
In enzymology, a formate dehydrogenase (cytochrome-c-553) () is an enzyme that catalyzes the chemical reaction :formate + ferricytochrome c-553 \rightleftharpoons CO2 + ferrocytochrome c-553 Thus, the two substrates of this enzyme are 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 ''Ull ... and ferricytochrome c-553, whereas its two products are CO2 and ferrocytochrome c-553. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with a cytochrome as acceptor. The systematic name of this enzyme class is formate:ferricytochrome-c-553 oxidoreductase. References * * EC 1.2.2 Enzymes of unknown structure {{1.2-enzyme-stub ...
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Formate Dehydrogenase (cytochrome)
In enzymology, a formate dehydrogenase (cytochrome) () is an enzyme that catalyzes the chemical reaction :formate + 2 ferricytochrome b1 \rightleftharpoons CO2 + 2 ferrocytochrome b1 + 2 H+ Thus, the two substrates of this enzyme are formate and ferricytochrome b1, whereas its 3 products are CO2, ferrocytochrome b1, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with a cytochrome as acceptor. The systematic name of this enzyme class is formate:ferricytochrome-b1 oxidoreductase. Other names in common use include formate dehydrogenase, and formate:cytochrome b1 oxidoreductase. This enzyme participates in glyoxylate and dicarboxylate metabolism Glyoxylate and dicarboxylate metabolism describes a variety of reactions involving glyoxylate or dicarboxylates. Glyoxylate is the conjugate base of glyoxylic acid, and within a buffered environment of known pH such as the cell cytoplasm these ter ... ...
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Colored Electron Tunneling F-DHN
''Colored'' (or ''coloured'') is a racial descriptor historically used in the United States during the Jim Crow, Jim Crow Era to refer to an African Americans, African American. In many places, it may be considered a Pejorative, slur, though it has taken on Coloureds, a special meaning in Southern Africa. Dictionary definitions The word ''colored'' (Middle English ''icoloured'') was first used in the 14th century but with a meaning other than race or ethnicity. The earliest uses of the term to denote a member of dark-skinned groups of peoples occurred in the second part of the 18th century in reference to South America. According to the ''Oxford English Dictionary'', "colored" was first used in this context in 1758 to translate the Spanish term ''mujeres de color'' ('colored women') in Antonio de Ulloa's ''A voyage to South America''. The term came in use in the United States during the early 19th century, and it then was adopted by emancipated slaves as a term of racial pride a ...
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Vitamin K2
Vitamin K2 or menaquinone (MK) () is one of three types of vitamin K, the other two being vitamin K1 (phylloquinone) and K3 (menadione). K2 is both a tissue and bacterial product (derived from vitamin K1 in both cases) and is usually found in animal products or fermented foods. The number ''n'' of isoprenyl units in their side chain differs and ranges from 4 to 13, hence Vitamin K2 consists of various forms. It is indicated as a suffix (-n), e. g. MK-7 or MK-9. The most common in the human diet is the short-chain, water-soluble menatetrenone (MK-4), which is usually produced by tissue and/or bacterial conversion of vitamin K1, and is commonly found in animal products. It is known that production of MK-4 from dietary plant vitamin K1 can be accomplished by animal tissues alone, as it proceeds in germ-free rodents. However, at least one published study concluded that "MK-4 present in food does not contribute to the vitamin K status as measured by serum vitamin K levels. MK-7, howe ...
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Cytochrome B
Cytochrome b within both molecular and cell biology, is a protein found in the mitochondria of eukaryotic cells. It functions as part of the electron transport chain and is the main subunit of transmembrane cytochrome bc1 and b6f complexes. Function In the mitochondrion of eukaryotes and in aerobic prokaryotes, cytochrome b is a component of respiratory chain complex III () — also known as the bc1 complex or ubiquinol-cytochrome c reductase. In plant chloroplasts and cyanobacteria, there is an analogous protein, cytochrome b6, a component of the plastoquinone-plastocyanin reductase (), also known as the b6f complex. These complexes are involved in electron transport, the pumping of protons to create a proton-motive force ( PMF). This proton gradient is used for the generation of ATP. These complexes play a vital role in cells. Structure Cytochrome b/b6 is an integral membrane protein of approximately 400 amino acid residues that probably has 8 transmembrane segments. ...
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Ferredoxin
Ferredoxins (from Latin ''ferrum'': iron + redox, often abbreviated "fd") are iron–sulfur proteins that mediate electron transfer in a range of metabolic reactions. The term "ferredoxin" was coined by D.C. Wharton of the DuPont Co. and applied to the "iron protein" first purified in 1962 by Mortenson, Valentine, and Carnahan from the anaerobic bacterium '' Clostridium pasteurianum''. Another redox protein, isolated from spinach chloroplasts, was termed "chloroplast ferredoxin". The chloroplast ferredoxin is involved in both cyclic and non-cyclic photophosphorylation reactions of photosynthesis. In non-cyclic photophosphorylation, ferredoxin is the last electron acceptor thus reducing the enzyme NADP+ reductase. It accepts electrons produced from sunlight- excited chlorophyll and transfers them to the enzyme ferredoxin: NADP+ oxidoreductase . Ferredoxins are small proteins containing iron and sulfur atoms organized as iron–sulfur clusters. These biological " capacitors" can ...
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