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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 hemoprotein, 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 el ...
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Cytochrome
Cytochromes are redox-active proteins containing a heme, with a central iron (Fe) atom at its core, as a cofactor. They are involved in the 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 na ...
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Reduction (chemistry)
Redox ( , , reduction–oxidation or oxidation–reduction) is a type of chemical reaction in which the oxidation states of the reactants change. Oxidation is the loss of electrons or an increase in the oxidation state, while reduction is the gain of electrons or a decrease in the oxidation state. The oxidation and reduction processes occur simultaneously in the chemical reaction. There are two classes of redox reactions: * Electron transfer, Electron-transfer – Only one (usually) electron flows from the atom, ion, or molecule being oxidized to the atom, ion, or molecule that is reduced. This type of redox reaction is often discussed in terms of redox couples and electrode potentials. * Atom transfer – An atom transfers from one Substrate (chemistry), substrate to another. For example, in the rusting of iron, the oxidation state of iron atoms increases as the iron converts to an oxide, and simultaneously, the oxidation state of oxygen decreases as it accepts electrons r ...
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Diazotroph
Diazotrophs are organisms capable of nitrogen fixation, i.e. converting the relatively inert diatomic nitrogen (N2) in Earth's atmosphere into bioavailable compound forms such as ammonia. Diazotrophs are typically microorganisms such as bacteria and archaea, with examples being rhizobia and '' Frankia'' and '' Azospirillum''. All diazotrophs contain iron-molybdenum or iron-vanadium nitrogenase systems, and two of the most studied systems are those of '' Klebsiella pneumoniae'' and '' Azotobacter vinelandii'' due to their genetic tractability and their fast growth. Etymology The word diazotroph is derived from the words ''diazo'' ("di" = two + "azo" = nitrogen) meaning "dinitrogen (N2)" and ''troph'' meaning "pertaining to food or nourishment", in summary dinitrogen utilizing. The word ''azote'' means nitrogen in French and was named by French chemist and biologist Antoine Lavoisier, who saw it as the part of air which cannot sustain life. Types Diazotrophs are scattered across B ...
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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. ''A. vinelandii'' also produces significant amounts of alginat ...
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Ubiquinol Oxidase (H+-transporting)
Ubiquinol oxidase (H+-transporting) (, ''cytochrome bb3 oxidase'', ''cytochrome bo oxidase'', ''cytochrome bd-I oxidase'') is an enzyme with systematic name ''ubiquinol:O2 oxidoreductase (H+-transporting)''. This enzyme catalyses the following chemical reaction : 2 ubiquinol + O2 + ''n'' H+in \rightleftharpoons 2 ubiquinone + 2 H2O + ''n'' H+out Ubiquinol oxidase contains a dinuclear centre comprising two hemes, or heme and copper Copper is a chemical element; it has symbol Cu (from Latin ) and atomic number 29. It is a soft, malleable, and ductile metal with very high thermal and electrical conductivity. A freshly exposed surface of pure copper has a pinkish-orang .... References External links * {{Portal bar, Biology, border=no EC 1.10.3 EC 7.1.1 ...
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Geobacillus
''Geobacillus'' is a bacterial genus from the family of Bacillaceae. Phylogeny The currently accepted taxonomy is based on the List of Prokaryotic names with Standing in Nomenclature (LPSN) and National Center for Biotechnology Information (NCBI). Unassigned species: * "''G. anatolicus''" Uysal et al. 2001 ex Caglayan & Bilgin 2011 * "''G. bogazici''" Turker et al. 2003 * "''G. kaue''" Uysal et al. 2001 ex Caglayan & Bilgin 2011 * "''G. mahadia''" Mohtar et al. 2016 * "''G. thermopakistaniensis''" Siddiqui et al. 2014 * "''G. thermoparaffinivorans''" Wang et al. 2005 * "''G. tropicalis''" Burgos-Figueroa et al. 2006 * "''G. uralicus''" Popova et al. 2002 See also * List of Bacteria genera * List of bacterial orders This article lists the orders of the Bacteria. The currently accepted taxonomy is based on the List of Prokaryotic names with Standing in Nomenclature (LPSN) and National Center for Biotechnology Information (NCBI) and the phylogeny is based on 16 ... References ...
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Pseudomonadota
Pseudomonadota (synonym "Proteobacteria") is a major phylum of gram-negative bacteria. Currently, they are considered the predominant phylum within the domain of bacteria. They are naturally found as pathogenic and free-living (non- parasitic) genera. The phylum comprises six classes ''Acidithiobacillia, Alphaproteobacteria, Betaproteobacteria, Gammaproteobacteria, Hydrogenophilia'', and '' Zetaproteobacteria.'' The Pseudomonadota are widely diverse, with differences in morphology, metabolic processes, relevance to humans, and ecological influence. Classification American microbiologist Carl Woese established this grouping in 1987, calling it informally the "purple bacteria and their relatives". The group was later formally named the 'Proteobacteria' after the Greek god Proteus, who was known to assume many forms. In 2021 the International Committee on Systematics of Prokaryotes designated the synonym Pseudomonadota, and renamed many other prokaryotic phyla as well. Th ...
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Respiratory Chain
An electron transport chain (ETC) is a series of protein complexes and other molecules which 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. Many of the enzymes in the electron transport chain are embedded within the membrane. 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 reactions are driven by the difference in the Gibbs free energy of reactants and products. The free energy released when a higher- ...
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Proton Pump
A proton pump is an integral membrane protein pump that builds up a proton gradient across a biological membrane. Proton pumps catalyze the following reaction: : n one side of a biological membrane/sub> + energy n the other side of the membrane/sub> Mechanisms are based on energy-induced 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, exhibiting different polypeptide compositions and evolutionary origins. Function Transport of the positively charged proton is typically electrogenic, i.e.: it generates an electric field across the membrane also called the membrane potential. Proton transport becomes electrogenic if not neutralized electrica ...
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Electron Spin
Spin is an intrinsic form of angular momentum carried by elementary particles, and thus by composite particles such as hadrons, atomic nuclei, and atoms. Spin is quantized, and accurate models for the interaction with spin require relativistic quantum mechanics or quantum field theory. The existence of electron spin angular momentum is inferred from experiments, such as the Stern–Gerlach experiment, in which silver atoms were observed to possess two possible discrete angular momenta despite having no orbital angular momentum. The relativistic spin–statistics theorem connects electron spin quantization to the Pauli exclusion principle: observations of exclusion imply half-integer spin, and observations of half-integer spin imply exclusion. Spin is described mathematically as a vector for some particles such as photons, and as a spinor or bispinor for other particles such as electrons. Spinors and bispinors behave similarly to vectors: they have definite magnitudes and ch ...
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High-spin Complex
In inorganic chemistry, crystal field theory (CFT) describes the breaking of degeneracies of electron orbital states, usually ''d'' or ''f'' orbitals, due to a static electric field produced by a surrounding charge distribution (anion neighbors). This theory has been used to describe various spectroscopies of transition metal coordination complexes, in particular optical spectra (colors). CFT successfully accounts for some magnetic properties, colors, hydration enthalpies, and spinel structures of transition metal complexes, but it does not attempt to describe bonding. CFT was developed by physicists Hans Bethe and John Hasbrouck van Vleck in the 1930s. CFT was subsequently combined with molecular orbital theory to form the more realistic and complex ligand field theory (LFT), which delivers insight into the process of chemical bonding in transition metal complexes. CFT can be complicated further by breaking assumptions made of relative metal and ligand orbital energies, requiring ...
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Active Site
In biology and biochemistry, the active site is the region of an enzyme where substrate molecules bind and undergo a chemical reaction. The active site consists of amino acid residues that form temporary bonds with the substrate, the ''binding site'', and residues that catalyse a reaction of that substrate, the ''catalytic site''. Although the active site occupies only ~10–20% of the volume of an enzyme, it is the most important part as it directly catalyzes the chemical reaction. It usually consists of three to four amino acids, while other amino acids within the protein are required to maintain the tertiary structure of the enzymes. Each active site is evolved to be optimised to bind a particular substrate and catalyse a particular reaction, resulting in high specificity. This specificity is determined by the arrangement of amino acids within the active site and the structure of the substrates. Sometimes enzymes also need to bind with some cofactors to fulfil their functio ...
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