Electron Bifurcation
In biochemistry, electron bifurcation (EB) refers to a system that enables an unfavorable (endergonic) transformation by coupling to a favorable (exergonic) transformation. Two electrons are involved: one flows to an acceptor with a "higher reduction potential and the other with a lower reduction potential" than the donor. The process is suspected of being common in bioenergetics. Two versions of EB are recognized. One involves redox of quinones and the other involves flavin group, flavins. Quinones and flavins are cofactors that are capable of undergoing 2 – 2 proton redox. A pervasive example of electron bifurcation is the Q cycle, which is part of the machinery that results in oxidative phosphorylation. In that case one electron from ubiquinol is directed to a Rieske cluster and the other electron is directed to a cytochrome b Cytochrome b within both molecular and cell biology, is a protein found in the mitochondria of eukaryotic cells. It functions as ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Biochemistry
Biochemistry or biological chemistry is the study of chemical processes within and relating to living organisms. A sub-discipline of both chemistry and biology, biochemistry may be divided into three fields: structural biology, enzymology and metabolism. Over the last decades of the 20th century, biochemistry has become successful at explaining living processes through these three disciplines. Almost all areas of the life sciences are being uncovered and developed through biochemical methodology and research.Voet (2005), p. 3. Biochemistry focuses on understanding the chemical basis which allows biological molecules to give rise to the processes that occur within living cells and between cells, Karp (2009), p. 2. in turn relating greatly to the understanding of tissues and organs, as well as organism structure and function. Miller (2012). p. 62. Biochemistry is closely related to molecular biology, which is the study of the molecular mechanisms of biological phenom ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Endergonic
In chemical thermodynamics, an endergonic reaction (; also called a heat absorbing nonspontaneous reaction or an unfavorable reaction) is a chemical reaction in which the standard change in free energy is positive, and an additional driving force is needed to perform this reaction. In layman's terms, the total amount of useful energy is negative (it takes more energy to start the reaction than what is received out of it) so the total energy is a net negative result. For an overall gain in the net result, see exergonic reaction. Another way to phrase this is that useful energy must be absorbed from the surroundings into the workable system for the reaction to happen. Under constant temperature and constant pressure conditions, this means that the change in the standard Gibbs free energy would be positive, :\Delta G^\circ > 0 for the reaction at standard state (i.e. at standard pressure (1 bar), and standard concentrations (1 molar) of all the reagents). In metabolism, an end ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Exergonic
An exergonic process is one which there is a positive flow of energy from the system to the surroundings. This is in contrast with an endergonic process. Constant pressure, constant temperature reactions are exergonic if and only if the Gibbs free energy change is negative (∆''G'' < 0). "Exergonic" (from the prefix exo-, derived for the Greek word ἔξω ''exō'', "outside" and the suffix -ergonic, derived from the Greek word ἔργον ''ergon'', " work") means "releasing energy in the form of work". In thermodynamics, work is defined as the energy moving from the system (the internal region) to the (the external region) during a given process. Al ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Quinone
The quinones are a class of organic compounds that are formally "derived from aromatic compounds benzene.html" ;"title="uch as benzene">uch as benzene or naphthalene] by conversion of an even number of –CH= groups into –C(=O)– groups with any necessary rearrangement of double bonds, resulting in "a fully Conjugated system, conjugated cyclic diketone, dione structure". The archetypical member of the class is 1,4-benzoquinone or cyclohexadienedione, often called simply "quinone" (thus the name of the class). Other important examples are 1,2-benzoquinone (''ortho''-quinone), 1,4-naphthoquinone and 9,10-anthraquinone. The name is derived from that of quinic acid (with the suffix "-one" indicating a ketone), since it is one of the compounds obtained upon oxidation of quinic acid. Quinic acid, like quinine is obtained from cinchona bark, called quinaquina in the indigenous languages of Peruvian tribes. Properties Quinones are oxidized derivatives of aromatic compounds and ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Flavin Group
Flavins (from Latin ''flavus'', "yellow") are organic compounds, like their base, pteridine. They are formed by the tricyclic heterocycle isoalloxazine. The biochemical source is the vitamin riboflavin. The flavin moiety is often attached with an adenosine diphosphate to form flavin adenine dinucleotide (FAD), and, in other circumstances, is found as flavin mononucleotide (or FMN), a phosphorylated form of riboflavin. It is in one or the other of these forms that flavin is present as a prosthetic group in flavoproteins. The flavin group is capable of undergoing oxidation-reduction reactions, and can accept either one electron in a two-step process or two electrons at once. Reduction is made with the addition of hydrogen atoms to specific nitrogen atoms on the isoalloxazine ring system: In aqueous solution, flavins are yellow-coloured when oxidized, taking a red colour in the semi-reduced anionic state or blue in the neutral ( semiquinone) state, and colourless when totally ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Cofactor (biochemistry)
A cofactor is a non-protein chemical compound or metallic ion that is required for an enzyme's role as a catalyst (a catalyst is a substance that increases the rate of a chemical reaction). Cofactors can be considered "helper molecules" that assist in biochemical transformations. The rates at which these happen are characterized in an area of study called enzyme kinetics. Cofactors typically differ from ligands in that they often derive their function by remaining bound. Cofactors can be divided into two types: inorganic ions and complex organic molecules called coenzymes. Coenzymes are mostly derived from vitamins and other organic essential nutrients in small amounts. (Note that some scientists limit the use of the term "cofactor" for inorganic substances; both types are included here.) Coenzymes are further divided into two types. The first is called a "prosthetic group", which consists of a coenzyme that is tightly (or even covalently) and permanently bound to a prote ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Q Cycle
The Q cycle (named for ''quinol'') describes a series of reactions that describe how the sequential oxidation and reduction of the lipophilic electron carrier, Coenzyme Q (CoQ), between the ubiquinol and ubiquinone forms, can result in the net movement of protons across a lipid bilayer (in the case of the mitochondria, the inner mitochondrial membrane). The Q cycle was first proposed by Peter D. Mitchell, though a modified version of Mitchell's original scheme is now accepted as the mechanism by which Complex III moves protons (i.e. how complex III contributes to the biochemical generation of the proton or pH, gradient, which is used for the biochemical generation of ATP). The first reaction of Q cycle is the 2-electron oxidation of ubiquinol by two oxidants, ''c1'' (Fe3+) and ubiquinone: : CoQH2 + cytochrome ''c1'' (Fe3+) + CoQ' → CoQ + CoQ'−• + cytochrome ''c1'' (Fe2+) + 2 H+ (intermembrane) The second reaction of the cycle involves the 2-electron oxidation of a second u ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Oxidative Phosphorylation
Oxidative phosphorylation (UK , US ) or electron transport-linked phosphorylation or terminal oxidation is the metabolic pathway in which cells use enzymes to oxidize nutrients, thereby releasing chemical energy in order to produce adenosine triphosphate (ATP). In eukaryotes, this takes place inside mitochondria. Almost all aerobic organisms carry out oxidative phosphorylation. This pathway is so pervasive because it releases more energy than alternative fermentation processes such as anaerobic glycolysis. The energy stored in the chemical bonds of glucose is released by the cell in the citric acid cycle producing carbon dioxide, and the energetic electron donors NADH and FADH. Oxidative phosphorylation uses these molecules and O2 to produce ATP, which is used throughout the cell whenever energy is needed. During oxidative phosphorylation, electrons are transferred from the electron donors to a series of electron acceptors in a series of redox reactions ending in oxygen, ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Ubiquinol
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 ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Rieske Protein
Rieske proteins are iron–sulfur protein (ISP) components of cytochrome ''bc''1 complexes and cytochrome b6f complexes and are responsible for electron transfer in some biological systems. John S. Rieske and co-workers first discovered the protein and in 1964 isolated an acetylated form of the bovine mitochondrial protein. In 1979 Trumpower's lab isolated the "oxidation factor" from bovine mitochondria and showed it was a reconstitutively-active form of the Rieske iron-sulfur protein It is a unique Fe-2Scluster in that one of the two Fe atoms is coordinated by two histidine residues rather than two cysteine residues. They have since been found in plants, animals, and bacteria with widely ranging electron reduction potentials from -150 to +400 mV. Biological function Ubiquinol-cytochrome-c reductase (also known as bc1 complex or complex III) is an enzyme complex of bacterial and mitochondrial oxidative phosphorylation systems. It catalyses the oxidation-reduction reacti ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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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 segm ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |
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Thermodynamic Processes
Classical thermodynamics considers three main kinds of thermodynamic process: (1) changes in a system, (2) cycles in a system, and (3) flow processes. (1)A Thermodynamic process is a process in which the thermodynamic state of a system is changed. A change in a system is defined by a passage from an initial to a final state of thermodynamic equilibrium. In classical thermodynamics, the actual course of the process is not the primary concern, and often is ignored. A state of thermodynamic equilibrium endures unchangingly unless it is interrupted by a thermodynamic operation that initiates a thermodynamic process. The equilibrium states are each respectively fully specified by a suitable set of thermodynamic state variables, that depend only on the current state of the system, not on the path taken by the processes that produce the state. In general, during the actual course of a thermodynamic process, the system may pass through physical states which are not describable as thermody ... [...More Info...]       [...Related Items...]     OR:     [Wikipedia]   [Google]   [Baidu]   |