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Cytochrome D
Cytochrome ''d'', previously known as cytochrome ''a''2, is a name for all cytochromes (electron-transporting heme proteins) that contain heme D as a cofactor. Two unrelated classes of cytochrome ''d'' are known: Cytochrome ''bd'', an enzyme that generates a charge across the membrane so that protons will move, and cytochrome ''cd1'' (NirS; SCOP ), a nitrite reductase. Cytochrome ''bd'' is found in plenty of aerobic bacteria, especially when it has grown with a limited oxygen supply. Compared to other terminal oxidases, it is notable for its high oxygen affinity and resistance to cyanide poisoning. It has a group of very similar relatives that do not use heme D, known as cyanide insensitive oxidases (CIOs). Function Cytochrome d is, as other proteins of its family, a membrane-bound hemeprotein, but unlike cytochromes a and b, cytochrome D has a heme D instead of a heme A or heme B group. Cytochrome d is part of the cytochrome bd terminal oxidase which catalyse the two e ... [...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 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Plastoquinone
Plastoquinone (PQ) is an isoprenoid quinone molecule involved in the electron transport chain in the light-dependent reactions of photosynthesis. The most common form of plastoquinone, known as PQ-A or PQ-9, is a 2,3-dimethyl-1,4-benzoquinone molecule with a side chain of nine isoprenyl units. There are other forms of plastoquinone, such as ones with shorter side chains like PQ-3 (which has 3 isoprenyl side units instead of 9) as well as analogs such as PQ-B, PQ-C, and PQ-D, which differ in their side chains. The benzoquinone and isoprenyl units are both nonpolar, anchoring the molecule within the inner section of a lipid bilayer, where the hydrophobic tails are usually found. Plastoquinones are very structurally similar to ubiquinone, or coenzyme Q10, differing by the length of the isoprenyl side chain, replacement of the methoxy groups with methyl groups, and removal of the methyl group in the 2 position on the quinone. Like ubiquinone, it can come in several oxidation sta ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Complexes
A protein complex or multiprotein complex is a group of two or more associated polypeptide chains. Protein complexes are distinct from multienzyme complexes, in which multiple catalytic domains are found in a single polypeptide chain. Protein complexes are a form of quaternary structure. Proteins in a protein complex are linked by non-covalent protein–protein interactions. These complexes are a cornerstone of many (if not most) biological processes. The cell is seen to be composed of modular supramolecular complexes, each of which performs an independent, discrete biological function. Through proximity, the speed and selectivity of binding interactions between enzymatic complex and substrates can be vastly improved, leading to higher cellular efficiency. Many of the techniques used to enter cells and isolate proteins are inherently disruptive to such large complexes, complicating the task of determining the components of a complex. Examples of protein complexes include the ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Homology (biology)
In biology, homology is similarity due to shared ancestry between a pair of structures or genes in different taxa. A common example of homologous structures is the forelimbs of vertebrates, where the wings of bats and birds, the arms of primates, the front flippers of whales and the forelegs of four-legged vertebrates like dogs and crocodiles are all derived from the same ancestral tetrapod structure. Evolutionary biology explains homologous structures adapted to different purposes as the result of descent with modification from a common ancestor. The term was first applied to biology in a non-evolutionary context by the anatomist Richard Owen in 1843. Homology was later explained by Charles Darwin's theory of evolution in 1859, but had been observed before this, from Aristotle onwards, and it was explicitly analysed by Pierre Belon in 1555. In developmental biology, organs that developed in the embryo in the same manner and from similar origins, such as from matching prim ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Electron Transport System
An electron transport chain (ETC) is a series of protein complexes and other molecules that electron transfer, transfer electrons from electron donors to electron acceptors via redox reactions (both Redox#Definitions, reduction and oxidation occurring simultaneously) and couples this electron transfer with the transfer of protons (H+ ions) across a biological membrane, membrane. The electrons that transferred from NADH and FADH2 to the ETC involves 4 multi-subunit large enzymes complexes and 2 mobile electron carriers. Many of the enzymes in the electron transport chain are membrane-bound. The flow of electrons through the electron transport chain is an exergonic process. The energy from the redox reactions creates an electrochemical gradient, electrochemical proton gradient that drives the synthesis of adenosine triphosphate (ATP). In Cellular respiration#Aerobic respiration, aerobic respiration, the flow of electrons terminates with molecular oxygen as the final electron accepto ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Aerobic Organisms
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Aerobic means "requiring air," in which "air" usually means oxygen. Aerobic may also refer to * Aerobic exercise, prolonged exercise of moderate intensity * Aerobics, a form of aerobic exercise * Aerobic respiration, the aerobic process of cellular respiration * Aerobic organism, a living thing with an oxygen-based metabolism See also * Anaerobic (other) Anaerobic means "living, active, occurring, or existing in the absence of free oxygen", as opposed to aerobic which means "living, active, or occurring only in the presence of oxygen." Anaerobic may also refer to: * Anaerobic adhesive, a bonding a ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nitrogen-fixing Bacteria
Nitrogen fixation is a chemical process by which molecular nitrogen (), with a strong triple covalent bond, in the air is converted into ammonia () or related nitrogenous compounds, typically in soil or aquatic systems but also in industry. Atmospheric nitrogen is molecular dinitrogen, a relatively nonreactive molecule that is metabolically useless to all but a few microorganisms. Biological nitrogen fixation or ''diazotrophy'' is an important microbials mediated process that converts dinitrogen (N2) gas to ammonia (NH3) using the nitrogenase protein complex (Nif). Nitrogen fixation is essential to life because fixed inorganic nitrogen compounds are required for the biosynthesis of all nitrogen-containing organic compounds, such as amino acids and proteins, nucleoside triphosphates and nucleic acids. As part of the nitrogen cycle, it is essential for agriculture and the manufacture of fertilizer. It is also, indirectly, relevant to the manufacture of all nitrogen chemical ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Azotobacter Vinelandii
''Azotobacter vinelandii'' is Gram-negative diazotroph that can fix nitrogen while grown aerobically. These bacteria are easily cultured and grown. ''A. vinelandii'' is a free-living N2 fixer known to produce many phytohormones and vitamins in soils. It produces fluorescent pyoverdine pigments. Nitrogenase The nitrogenase holoenzyme of ''A. vinelandii'' has been characterised by X-ray crystallography in both ADP tetrafluoroaluminate-bound and Mg ATP-bound states. The enzyme possesses molybdenum iron- sulfido cluster cofactors (FeMoco) as active sites, each bearing two pseudocubic iron-sulfido structures. Applications It is a genetically tractable system that is used to study nitrogen fixation. Genetically engineered strains can produce significantly higher amounts of ammonia. Appropriate ammonia emissions can provide crops with the ammonia they need without excess amounts that can pollute lakes and oceans. Variable ploidy ''A. vinelandii'' can contain up to 80 chr ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ubiquinol Oxidase (H+-transporting)
A ubiquinol is an electron-rich (reduced) form of coenzyme Q (ubiquinone). The term most often refers to ubiquinol-10, with a 10-unit tail most commonly found in humans. The natural ubiquinol form of coenzyme Q is 2,3-dimethoxy-5-methyl-6-poly prenyl-1,4-benzoquinol, where the polyprenylated side-chain is 9-10 units long in mammals. Coenzyme Q10 (CoQ10) exists in three redox states, fully oxidized (ubiquinone), partially reduced (semiquinone or ubisemiquinone), and fully reduced (ubiquinol). The redox functions of ubiquinol in cellular energy production and antioxidant protection are based on the ability to exchange two electrons in a redox cycle between ubiquinol (reduced) and the ubiquinone (oxidized) form. Characteristics Because humans can synthesize ubiquinol, it is not classed as a vitamin. Bioavailability It is well-established that CoQ10 is not well absorbed into the body, as has been published in many peer-reviewed scientific journals. Since the ubiquinol form has tw ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Geobacillus
''Geobacillus'' is a bacterial genus from the family of Bacillaceae The Bacillaceae are a family of gram-positive, heterotrophic, rod-shaped bacteria that may produce endospores. Motile members of this family are characterized by peritrichous flagella. Some Bacillaceae are aerobic, while others are facultative o .... References Further reading * * * * * Bacillaceae Bacteria genera {{Firmicutes-stub ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Respiratory Chain
An electron transport chain (ETC) is a series of protein complexes and other molecules that transfer electrons from electron donors to electron acceptors via redox reactions (both reduction and oxidation occurring simultaneously) and couples this electron transfer with the transfer of protons (H+ ions) across a membrane. The electrons that transferred from NADH and FADH2 to the ETC involves 4 multi-subunit large enzymes complexes and 2 mobile electron carriers. Many of the enzymes in the electron transport chain are membrane-bound. The flow of electrons through the electron transport chain is an exergonic process. The energy from the redox reactions creates an electrochemical proton gradient that drives the synthesis of adenosine triphosphate (ATP). In aerobic respiration, the flow of electrons terminates with molecular oxygen as the final electron acceptor. In anaerobic respiration, other electron acceptors are used, such as sulfate. In an electron transport chain, the redox r ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Proton Pump
A proton pump is an integral membrane protein pump that builds up a proton gradient across a biological membrane A biological membrane, biomembrane or cell membrane is a selectively permeable membrane that separates the interior of a cell from the external environment or creates intracellular compartments by serving as a boundary between one part of the .... Proton pumps catalyze the following reaction: :[on one side of a biological membrane] + energy [on the other side of the membrane] Mechanisms are based on energy-induced Protein conformation, conformational changes of the protein structure or on the Q cycle. During evolution, proton pumps have arisen independently on multiple occasions. Thus, not only throughout nature but also within single cells, different proton pumps that are evolutionarily unrelated can be found. Proton pumps are divided into different major classes of pumps that use different sources of energy, have different polypeptide compositions and evol ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
