An antibiotic substance produced by Streptomyces species. It inhibits mitochondrial respiration and may deplete cellular levels of ATP. Antimycin A1 has been used as a fungicide, insecticide, and miticide. (From Merck Index, 12th ed)
A multisubunit enzyme complex that contains CYTOCHROME B GROUP; CYTOCHROME C1; and iron-sulfur centers. It catalyzes the oxidation of ubiquinol to UBIQUINONE, and transfers the electrons to CYTOCHROME C. In MITOCHONDRIA the redox reaction is coupled to the transport of PROTONS across the inner mitochondrial membrane.
A botanical insecticide that is an inhibitor of mitochondrial electron transport.
The process by which ELECTRONS are transported from a reduced substrate to molecular OXYGEN. (From Bennington, Saunders Dictionary and Encyclopedia of Laboratory Medicine and Technology, 1984, p270)
The 8-hydroxy derivatives inhibit various enzymes and their halogenated derivatives, though neurotoxic, are used as topical anti-infective agents, among other uses.
Inorganic salts of HYDROGEN CYANIDE containing the -CN radical. The concept also includes isocyanides. It is distinguished from NITRILES, which denotes organic compounds containing the -CN radical.
A lipid-soluble benzoquinone which is involved in ELECTRON TRANSPORT in mitochondrial preparations. The compound occurs in the majority of aerobic organisms, from bacteria to higher plants and animals.
Acrylic acids or acrylates which are substituted in the C-2 position with a methyl group.
Semiautonomous, self-reproducing organelles that occur in the cytoplasm of all cells of most, but not all, eukaryotes. Each mitochondrion is surrounded by a double limiting membrane. The inner membrane is highly invaginated, and its projections are called cristae. Mitochondria are the sites of the reactions of oxidative phosphorylation, which result in the formation of ATP. They contain distinctive RIBOSOMES, transfer RNAs (RNA, TRANSFER); AMINO ACYL T RNA SYNTHETASES; and elongation and termination factors. Mitochondria depend upon genes within the nucleus of the cells in which they reside for many essential messenger RNAs (RNA, MESSENGER). Mitochondria are believed to have arisen from aerobic bacteria that established a symbiotic relationship with primitive protoeukaryotes. (King & Stansfield, A Dictionary of Genetics, 4th ed)
A closely related group of toxic substances elaborated by various strains of Streptomyces. They are 26-membered macrolides with lactone moieties and double bonds and inhibit various ATPases, causing uncoupling of phosphorylation from mitochondrial respiration. Used as tools in cytochemistry. Some specific oligomycins are RUTAMYCIN, peliomycin, and botrycidin (formerly venturicidin X).
Derivatives of SUCCINIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain a 1,4-carboxy terminated aliphatic structure.
Hemeproteins whose characteristic mode of action involves transfer of reducing equivalents which are associated with a reversible change in oxidation state of the prosthetic group. Formally, this redox change involves a single-electron, reversible equilibrium between the Fe(II) and Fe(III) states of the central iron atom (From Enzyme Nomenclature, 1992, p539). The various cytochrome subclasses are organized by the type of HEME and by the wavelength range of their reduced alpha-absorption bands.
Chemical agents that uncouple oxidation from phosphorylation in the metabolic cycle so that ATP synthesis does not occur. Included here are those IONOPHORES that disrupt electron transfer by short-circuiting the proton gradient across mitochondrial membranes.
NAD(P)H:(quinone acceptor) oxidoreductases. A family that includes three enzymes which are distinguished by their sensitivity to various inhibitors. EC 1.6.99.2 (NAD(P)H DEHYDROGENASE (QUINONE);) is a flavoprotein which reduces various quinones in the presence of NADH or NADPH and is inhibited by dicoumarol. EC 1.6.99.5 (NADH dehydrogenase (quinone)) requires NADH, is inhibited by AMP and 2,4-dinitrophenol but not by dicoumarol or folic acid derivatives. EC 1.6.99.6 (NADPH dehydrogenase (quinone)) requires NADPH and is inhibited by dicoumarol and folic acid derivatives but not by 2,4-dinitrophenol.
Cytochromes (electron-transporting proteins) with protoheme (HEME B) as the prosthetic group.
A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).
A barbiturate with hypnotic and sedative properties (but not antianxiety). Adverse effects are mainly a consequence of dose-related CNS depression and the risk of dependence with continued use is high. (From Martindale, The Extra Pharmacopoeia, 30th ed, p565)
The rate at which oxygen is used by a tissue; microliters of oxygen STPD used per milligram of tissue per hour; the rate at which oxygen enters the blood from alveolar gas, equal in the steady state to the consumption of oxygen by tissue metabolism throughout the body. (Stedman, 25th ed, p346)
A water-soluble, colorless crystal with an acid taste that is used as a chemical intermediate, in medicine, the manufacture of lacquers, and to make perfume esters. It is also used in foods as a sequestrant, buffer, and a neutralizing agent. (Hawley's Condensed Chemical Dictionary, 12th ed, p1099; McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed, p1851)
A highly poisonous compound that is an inhibitor of many metabolic processes, but has been shown to be an especially potent inhibitor of heme enzymes and hemeproteins. It is used in many industrial processes.
Mitochondria in hepatocytes. As in all mitochondria, there are an outer membrane and an inner membrane, together creating two separate mitochondrial compartments: the internal matrix space and a much narrower intermembrane space. In the liver mitochondrion, an estimated 67% of the total mitochondrial proteins is located in the matrix. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p343-4)
A genus of gram-negative bacteria widely distributed in fresh water as well as marine and hypersaline habitats.
A proton ionophore that is commonly used as an uncoupling agent in biochemical studies.
Chelating agent and inhibitor of cellular respiration.
The 30-kDa membrane-bound c-type cytochrome protein of mitochondria that functions as an electron donor to CYTOCHROME C GROUP in the mitochondrial and bacterial RESPIRATORY CHAIN. (From Enzyme Nomenclature, 1992, p545)
A proton ionophore. It is commonly used as an uncoupling agent and inhibitor of photosynthesis because of its effects on mitochondrial and chloroplast membranes.
The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)
Inorganic salts of the hypothetical acid, H3Fe(CN)6.
Organic compounds that contain two nitro groups attached to a phenol.
Thiazoles are heterocyclic organic compounds containing a sulfur atom and a nitrogen atom, which are bound by two carbon atoms to form a five-membered ring, and are widely found in various natural and synthetic substances, including some pharmaceuticals and vitamins.
An anti-gas warfare agent that is effective against Lewisite (dichloro(2-chlorovinyl)arsine) and formerly known as British Anti-Lewisite or BAL. It acts as a chelating agent and is used in the treatment of arsenic, gold, and other heavy metal poisoning.
The various filaments, granules, tubules or other inclusions within mitochondria.
A flavoprotein and iron sulfur-containing oxidoreductase that catalyzes the oxidation of NADH to NAD. In eukaryotes the enzyme can be found as a component of mitochondrial electron transport complex I. Under experimental conditions the enzyme can use CYTOCHROME C GROUP as the reducing cofactor. The enzyme was formerly listed as EC 1.6.2.1.
Molecules or ions formed by the incomplete one-electron reduction of oxygen. These reactive oxygen intermediates include SINGLET OXYGEN; SUPEROXIDES; PEROXIDES; HYDROXYL RADICAL; and HYPOCHLOROUS ACID. They contribute to the microbicidal activity of PHAGOCYTES, regulation of signal transduction and gene expression, and the oxidative damage to NUCLEIC ACIDS; PROTEINS; and LIPIDS.
The mitochondria of the myocardium.
The metabolic process of all living cells (animal and plant) in which oxygen is used to provide a source of energy for the cell.
Electron transfer through the cytochrome system liberating free energy which is transformed into high-energy phosphate bonds.
An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.
A pre-emergent herbicide.
The art or process of comparing photometrically the relative intensities of the light in different parts of the spectrum.
A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed)
Drugs that are chemically similar to naturally occurring metabolites, but differ enough to interfere with normal metabolic pathways. (From AMA Drug Evaluations Annual, 1994, p2033)
A group of cytochromes with covalent thioether linkages between either or both of the vinyl side chains of protoheme and the protein. (Enzyme Nomenclature, 1992, p539)
A group of oxidoreductases that act on NADH or NADPH. In general, enzymes using NADH or NADPH to reduce a substrate are classified according to the reverse reaction, in which NAD+ or NADP+ is formally regarded as an acceptor. This subclass includes only those enzymes in which some other redox carrier is the acceptor. (Enzyme Nomenclature, 1992, p100) EC 1.6.
Amides of salicylic acid.
The rate dynamics in chemical or physical systems.
A strong oxidizing agent used in aqueous solution as a ripening agent, bleach, and topical anti-infective. It is relatively unstable and solutions deteriorate over time unless stabilized by the addition of acetanilide or similar organic materials.
Inorganic salts of the hypothetical acid ferrocyanic acid (H4Fe(CN)6).
Cytochromes of the b group that have alpha-band absorption of 563-564 nm. They occur as subunits in MITOCHONDRIAL ELECTRON TRANSPORT COMPLEX III.

Characterization of a leukotriene C4 export mechanism in human platelets: possible involvement of multidrug resistance-associated protein 1. (1/715)

Platelets express leukotriene (LT) C4 synthase and can thus participate in the formation of bioactive LTC4. To further elucidate the relevance of this capability, we have now determined the capacity of human platelets to export LTC4. Endogenously formed LTC4 was efficiently released from human platelets after incubation with LTA4 at 37 degrees C, whereas only 15% of produced LTC4 was exported when the cells were incubated at 0 degrees C. The activation energy of the process was calculated to 49.9 +/- 7.7 kJ/mol, indicating carrier-mediated LTC4 export. This was also supported by the finding that the transport was saturable, reaching a maximal export rate of 470 +/- 147 pmol LTC4/min x 10(9) platelets. Furthermore, markedly suppressed LTC4 transport was induced by a combination of the metabolic inhibitors antimycin A and 2-deoxyglucose, suggesting energy-dependent export. The presence in platelets of multidrug resistance-associated protein 1 (MRP1), a protein described to be an energy-dependent LTC4 transporter in various cell types, was demonstrated at the mRNA and protein level. Additional support for a role of MRP1 in platelet LTC4 export was obtained by the findings that the process was inhibited by probenecid and the 5-lipoxygenase-activating protein (FLAP) inhibitor, MK-886. The present findings further support the physiological relevance of platelet LTC4 production.  (+info)

Ubiquinol:cytochrome c oxidoreductase. Effects of inhibitors on reverse electron transfer from the iron-sulfur protein to cytochrome b. (2/715)

The effects of inhibitors on the reduction of the bis-heme cytochrome b of ubiquinol: cytochrome c oxidoreductase (complex III, bc1 complex) has been studied in bovine heart submitochondrial particles (SMP) when cytochrome b was reduced by NADH and succinate via the ubiquinone (Q) pool or by ascorbate plus N,N,N', N'-tetramethyl-p-phenylenediamine via cytochrome c1 and the iron-sulfur protein of complex III (ISP). The inhibitors used were antimycin (an N-side inhibitor), beta-methoxyacrylate derivatives, stigmatellin (P-side inhibitors), and ethoxyformic anhydride, which modifies essential histidyl residues in ISP. In agreement with our previous findings, the following results were obtained: (i) When ISP/cytochrome c1 were prereduced or SMP were treated with a P-side inhibitor, the high potential heme bH was fully and rapidly reduced by NADH or succinate, whereas the low potential heme bL was only partially reduced. (ii) Reverse electron transfer from ISP/c1 to cytochrome b was inhibited more by antimycin than by the P-side inhibitors. This reverse electron transfer was unaffected when, instead of normal SMP, Q-extracted SMP containing 200-fold less Q (0. 06 mol Q/mol cytochrome b or c1) were used. (iii) The cytochrome b reduced by reverse electron transfer through the leak of a P-side inhibitor was rapidly oxidized upon subsequent addition of antimycin. This antimycin-induced reoxidation did not happen when Q-extracted SMP were used. The implications of these results on the path of electrons in complex III, on oxidant-induced extra cytochrome b reduction, and on the inhibition of forward electron transfer to cytochrome b by a P-side plus an N-side inhibitor have been discussed.  (+info)

Light-induced oxidation-reduction reactions of cytochromes in the green sulfur photosynthetic bacterium Prosthecochloris aesturarii. (3/715)

The light-induced oxidation-reduction reactions of cytochromes in intact cells, starved cells, and chlorobium vesicle fractions of the green sulfur photosynthetic bacterium Prosthecochloris aesturarii were studied under anaerobic conditions. On the basis of both kinetic and spectral properties, at least three cytochrome species were found to be involved in the light-induced oxidation-reduction reactions of intact cells. These cytochromes were designated according to the positions of alpha-band maxima as C555 (rapid and slow components) and C552 (intermediate). By comparing the light-minus-dark difference spectra with the reduced-minus-oxidized difference spectra of purified cytochromes of this organism, rapid component C555 and intermediate component C552 are suggested to correspond to the purified cytochromes c-555(550) and c-551.5, respectively. Although the identity of the slow-phase component is uncertain, one possibility is that the slow phase is due to the bound form of c-555(550). In substrate-depleted (starved) cells, only one cytochrome species, C555 remained in the reduced state in the dark and oxidized upon actinic illumination. This corresponds to the rapid C555 component in intact cells. In the case of chlorobium vesicle fractions, one cytochrome species having an alpha-band maximum at 554 nm was oxidized by actinic light. The effects of several inhibitors on the absorbance changes of intact cells were studied. Antimycin A decreased the rate of the dark reduction of rapid C555 component. The complex effects of CCCP (carbonyl cyanide m-chlorophenylhydrazone) on the oxidation-reduction reactions of cytochromes were interpreted as the results of inhibition of the electron donation to oxidized C552 and C555 (slow), and a shift of the dark steady-state redox levels of cytochromes. Based on these findings, it is suggested that the rapid C555 component is located in a cyclic electron transfer pathway. The other two cytochromes, C552 and C555 (slow), may be located in non-cyclic electron transfer pathways and receive electrons from exogenous substrates such as sodium sulfide. A tentative scheme for the electron transfer system in Prosthecochloris aestuarii is presented and its nature is discussed.  (+info)

Roles of Na(+)-Ca2+ exchange and of mitochondria in the regulation of presynaptic Ca2+ and spontaneous glutamate release. (4/715)

The release of neurotransmitter from presynaptic terminals depends on an increase in the intracellular Ca2+ concentration ([Ca2+]i). In addition to the opening of presynaptic Ca2+ channels during excitation, other Ca2+ transport systems may be involved in changes in [Ca2+]i. We have studied the regulation of [Ca2+]i in nerve terminals of hippocampal cells in culture by the Na(+)-Ca2+ exchanger and by mitochondria. In addition, we have measured changes in the frequency of spontaneous excitatory postsynaptic currents (sEPSC) before and after the inhibition of the exchanger and of mitochondrial metabolism. We found rather heterogeneous [Ca2+]i responses of individual presynaptic terminals after inhibition of Na(+)-Ca2+ exchange. The increase in [Ca2+]i became more uniform and much larger after additional treatment of the cells with mitochondrial inhibitors. Correspondingly, sEPSC frequencies changed very little when only Na(+)-Ca2+ exchange was inhibited, but increased dramatically after additional inhibition of mitochondria. Our results provide evidence for prominent roles of Na(+)-Ca2+ exchange and mitochondria in presynaptic Ca2+ regulation and spontaneous glutamate release.  (+info)

Interorganelle signaling is a determinant of longevity in Saccharomyces cerevisiae. (5/715)

Replicative capacity, which is the number of times an individual cell divides, is the measure of longevity in the yeast Saccharomyces cerevisiae. In this study, a process that involves signaling from the mitochondrion to the nucleus, called retrograde regulation, is shown to determine yeast longevity, and its induction resulted in postponed senescence. Activation of retrograde regulation, by genetic and environmental means, correlated with increased replicative capacity in four different S. cerevisiae strains. Deletion of a gene required for the retrograde response, RTG2, eliminated the increased replicative capacity. RAS2, a gene previously shown to influence longevity in yeast, interacts with retrograde regulation in setting yeast longevity. The molecular mechanism of aging elucidated here parallels the results of genetic studies of aging in nematodes and fruit flies, as well as the caloric restriction paradigm in mammals, and it underscores the importance of metabolic regulation in aging, suggesting a general applicability.  (+info)

Oxygen sensing in yeast: evidence for the involvement of the respiratory chain in regulating the transcription of a subset of hypoxic genes. (6/715)

Oxygen availability affects the transcription of a number of genes in nearly all organisms. Although the molecular mechanisms for sensing oxygen are not precisely known, heme is thought to play a pivotal role. Here, we address the possibility that oxygen sensing in yeast, as in mammals, involves a redox-sensitive hemoprotein. We have found that carbon monoxide (CO) completely blocks the anoxia-induced expression of two hypoxic genes, OLE1 and CYC7, partially blocks the induction of a third gene, COX5b, and has no effect on the expression of other hypoxic or aerobic genes. In addition, transition metals (Co and Ni) induce the expression of OLE1 and CYC7 in a concentration-dependent manner under aerobic conditions. These findings suggest that the redox state of an oxygen-binding hemoprotein is involved in controlling the expression of at least two hypoxic yeast genes. By using mutants deficient in each of the two major yeast CO-binding hemoproteins (cytochrome c oxidase and flavohemoglobin), respiratory inhibitors, and cob1 and rho0 mutants, we have found that the respiratory chain is involved in the anoxic induction of these two genes and that cytochrome c oxidase is likely the hemoprotein "sensor." Our findings also indicate that there are at least two classes of hypoxic genes in yeast (CO sensitive and CO insensitive) and imply that multiple pathways/mechanisms are involved in modulating the expression of hypoxic yeast genes.  (+info)

Role of tyrosine phosphorylation in the reassembly of occludin and other tight junction proteins. (7/715)

After the simulation of anoxia by ATP depletion of MDCK cell monolayers with metabolic inhibitors, the tight junction (TJ) is known to become structurally perturbed, leading to loss of the permeability barrier. Peripheral TJ proteins such as zonula occludens 1 (ZO-1), ZO-2, and cingulin become extremely insoluble and associate into large macromolecular complexes (T. Tsukamoto and S. K. Nigam. J. Biol. Chem. 272: 16133-16139, 1997). For up to 3 h, this process is reversible by ATP repletion. We now show that the reassembly process depends on tyrosine phosphorylation. Recovery of transepithelial electrical resistance in ATP-replete monolayers was markedly inhibited by the tyrosine kinase inhibitor, genistein. Indirect immunofluorescence revealed a decrease in staining of occludin, a membrane component of the TJ, in the region of the TJ after ATP depletion, which reversed after ATP repletion; this reversal process was inhibited by genistein. Examination of the Triton X-100 solubilities of occludin and several nonmembrane TJ proteins revealed a shift of occludin and nonmembrane TJ proteins into an insoluble pool following ATP depletion. These changes reversed after ATP repletion, and the movement of insoluble occludin, ZO-1, and ZO-2 back into the soluble pool was again via a genistein-sensitive mechanism. Rate-zonal centrifugation analyses of detergent-soluble TJ proteins showed a reversible increase in higher density fractions following ATP depletion-repletion, although this change was not affected by genistein. In 32P-labeled cells, dephosphorylation of all studied TJ proteins was observed during ATP depletion, followed by rephosphorylation during ATP repletion; rephosphorylation of occludin was inhibited by genistein. Furthermore, during the ATP repletion phase, tyrosine phosphorylation of Triton X-100-insoluble occludin, which is localized at the junction, as well as ZO-2, p130/ZO-3 (though not ZO-1), and other proteins was evident; this tyrosine phosphorylation was completely inhibited by genistein. This indicates that tyrosine kinase activity is necessary for TJ reassembly during ATP repletion and suggests an important role for the tyrosine phosphorylation of occludin, ZO-2, p130/ZO-3, and possibly other proteins in the processes involved in TJ (re)formation.  (+info)

A mechanism for the synergistic antimalarial action of atovaquone and proguanil. (8/715)

A combination of atovaquone and proguanil has been found to be quite effective in treating malaria, with little evidence of the emergence of resistance when atovaquone was used as a single agent. We have examined possible mechanisms for the synergy between these two drugs. While proguanil by itself had no effect on electron transport or mitochondrial membrane potential (DeltaPsim), it significantly enhanced the ability of atovaquone to collapse DeltaPsim when used in combination. This enhancement was observed at pharmacologically achievable doses. Proguanil acted as a biguanide rather than as its metabolite cycloguanil (a parasite dihydrofolate reductase [DHFR] inhibitor) to enhance the atovaquone effect; another DHFR inhibitor, pyrimethamine, also had no enhancing effect. Proguanil-mediated enhancement was specific for atovaquone, since the effects of other mitochondrial electron transport inhibitors, such as myxothiazole and antimycin, were not altered by inclusion of proguanil. Surprisingly, proguanil did not enhance the ability of atovaquone to inhibit mitochondrial electron transport in malaria parasites. These results suggest that proguanil in its prodrug form acts in synergy with atovaquone by lowering the effective concentration at which atovaquone collapses DeltaPsim in malaria parasites. This could explain the paradoxical success of the atovaquone-proguanil combination even in regions where proguanil alone is ineffective due to resistance. The results also suggest that the atovaquone-proguanil combination may act as a site-specific uncoupler of parasite mitochondria in a selective manner.  (+info)

Antimycin A is an antibiotic substance produced by various species of Streptomyces bacteria. It is known to inhibit the electron transport chain in mitochondria, which can lead to cellular dysfunction and death. Antimycin A has been used in research to study the mechanisms of cellular respiration and oxidative phosphorylation.

In a medical context, antimycin A is not used as a therapeutic agent due to its toxicity to mammalian cells. However, it may be used in laboratory settings to investigate various biological processes or to develop new therapies for diseases related to mitochondrial dysfunction.

Electron Transport Complex III, also known as cytochrome bc1 complex or ubiquinol-cytochrome c reductase, is a protein complex located in the inner mitochondrial membrane of eukaryotic cells and the cytoplasmic membrane of prokaryotic cells. It plays a crucial role in the electron transport chain (ETC), a series of complexes that generate energy in the form of ATP through a process called oxidative phosphorylation.

In ETC, Electron Transport Complex III accepts electrons from ubiquinol and transfers them to cytochrome c. This electron transfer is coupled with the translocation of protons (H+ ions) across the membrane, creating an electrochemical gradient. The energy stored in this gradient drives the synthesis of ATP by ATP synthase.

Electron Transport Complex III consists of several subunits, including cytochrome b, cytochrome c1, and the Rieske iron-sulfur protein. These subunits work together to facilitate the electron transfer and proton translocation processes.

Rotenone is not strictly a medical term, but it is a pesticide that is used in some medical situations. According to the National Pesticide Information Center, rotenone is a pesticide derived from the roots and stems of several plants, including Derris Eliptica, Lonchocarpus utilis, and Tephrosia vogelii. It is used as a pesticide to control insects, mites, and fish in both agricultural and residential settings.

In medical contexts, rotenone has been studied for its potential effects on human health, particularly in relation to Parkinson's disease. Some research suggests that exposure to rotenone may increase the risk of developing Parkinson's disease, although more studies are needed to confirm this link. Rotenone works by inhibiting the mitochondria in cells, which can lead to cell death and neurodegeneration.

It is important to note that rotenone is highly toxic and should be handled with care. It can cause skin and eye irritation, respiratory problems, and gastrointestinal symptoms if ingested or inhaled. Therefore, it is recommended to use personal protective equipment when handling rotenone and to follow all label instructions carefully.

The Electron Transport Chain (ETC) is a series of complexes in the inner mitochondrial membrane that are involved in the process of cellular respiration. It is the final pathway for electrons derived from the oxidation of nutrients such as glucose, fatty acids, and amino acids to be transferred to molecular oxygen. This transfer of electrons drives the generation of a proton gradient across the inner mitochondrial membrane, which is then used by ATP synthase to produce ATP, the main energy currency of the cell.

The electron transport chain consists of four complexes (I-IV) and two mobile electron carriers (ubiquinone and cytochrome c). Electrons from NADH and FADH2 are transferred to Complex I and Complex II respectively, which then pass them along to ubiquinone. Ubiquinone then transfers the electrons to Complex III, which passes them on to cytochrome c. Finally, cytochrome c transfers the electrons to Complex IV, where they combine with oxygen and protons to form water.

The transfer of electrons through the ETC is accompanied by the pumping of protons from the mitochondrial matrix to the intermembrane space, creating a proton gradient. The flow of protons back across the inner membrane through ATP synthase drives the synthesis of ATP from ADP and inorganic phosphate.

Overall, the electron transport chain is a crucial process for generating energy in the form of ATP in the cell, and it plays a key role in many metabolic pathways.

Hydroxyquinolines are a group of synthetic antimicrobial agents that contain a hydroxyl group (-OH) attached to a quinoline ring. They have been used in the treatment of various bacterial, fungal, and parasitic infections. Some common examples of hydroxyquinolines include chloroquine, hydroxychloroquine, and quinacrine. These agents work by inhibiting the growth and multiplication of microorganisms, although their exact mechanisms of action may vary. Chloroquine and hydroxychloroquine, for example, are known to interfere with the replication of the malaria parasite within red blood cells, while quinacrine has been used to treat certain types of protozoal infections.

It is important to note that the use of hydroxyquinolines is associated with a number of potential side effects and risks, including gastrointestinal disturbances, visual disturbances, and cardiac toxicity. As such, they should only be used under the close supervision of a healthcare professional.

Cyanides are a group of chemical compounds that contain the cyano group, -CN, which consists of a carbon atom triple-bonded to a nitrogen atom. They are highly toxic and can cause rapid death due to the inhibition of cellular respiration. Cyanide ions (CN-) bind to the ferric iron in cytochrome c oxidase, a crucial enzyme in the electron transport chain, preventing the flow of electrons and the production of ATP, leading to cellular asphyxiation.

Common sources of cyanides include industrial chemicals such as hydrogen cyanide (HCN) and potassium cyanide (KCN), as well as natural sources like certain fruits, nuts, and plants. Exposure to high levels of cyanides can occur through inhalation, ingestion, or skin absorption, leading to symptoms such as headache, dizziness, nausea, vomiting, rapid heartbeat, seizures, coma, and ultimately death. Treatment for cyanide poisoning typically involves the use of antidotes that bind to cyanide ions and convert them into less toxic forms, such as thiosulfate and rhodanese.

Ubiquinone, also known as coenzyme Q10 (CoQ10), is a lipid-soluble benzoquinone that plays a crucial role in the mitochondrial electron transport chain as an essential component of Complexes I, II, and III. It functions as an electron carrier, assisting in the transfer of electrons from reduced nicotinamide adenine dinucleotide (NADH) and flavin adenine dinucleotide (FADH2) to molecular oxygen during oxidative phosphorylation, thereby contributing to the generation of adenosine triphosphate (ATP), the primary energy currency of the cell.

Additionally, ubiquinone acts as a potent antioxidant in both membranes and lipoproteins, protecting against lipid peroxidation and oxidative damage to proteins and DNA. Its antioxidant properties stem from its ability to donate electrons and regenerate other antioxidants like vitamin E. Ubiquinone is synthesized endogenously in all human cells, with the highest concentrations found in tissues with high energy demands, such as the heart, liver, kidneys, and skeletal muscles.

Deficiency in ubiquinone can result from genetic disorders, aging, or certain medications (such as statins), leading to impaired mitochondrial function and increased oxidative stress. Supplementation with ubiquinone has been explored as a potential therapeutic strategy for various conditions associated with mitochondrial dysfunction and oxidative stress, including cardiovascular diseases, neurodegenerative disorders, and cancer.

Methacrylates are a group of chemical compounds that contain the methacrylate functional group, which is a vinyl group (CH2=CH-) with a carbonyl group (C=O) at the β-position. This structure gives them unique chemical and physical properties, such as low viscosity, high reactivity, and resistance to heat and chemicals.

In medical terms, methacrylates are used in various biomedical applications, such as dental restorative materials, bone cements, and drug delivery systems. For example, methacrylate-based resins are commonly used in dentistry for fillings, crowns, and bridges due to their excellent mechanical properties and adhesion to tooth structures.

However, there have been concerns about the potential toxicity of methacrylates, particularly their ability to release monomers that can cause allergic reactions, irritation, or even mutagenic effects in some individuals. Therefore, it is essential to use these materials with caution and follow proper handling and safety protocols.

Mitochondria are specialized structures located inside cells that convert the energy from food into ATP (adenosine triphosphate), which is the primary form of energy used by cells. They are often referred to as the "powerhouses" of the cell because they generate most of the cell's supply of chemical energy. Mitochondria are also involved in various other cellular processes, such as signaling, differentiation, and apoptosis (programmed cell death).

Mitochondria have their own DNA, known as mitochondrial DNA (mtDNA), which is inherited maternally. This means that mtDNA is passed down from the mother to her offspring through the egg cells. Mitochondrial dysfunction has been linked to a variety of diseases and conditions, including neurodegenerative disorders, diabetes, and aging.

Oligomycins are a group of antibiotics produced by various species of Streptomyces bacteria. They are characterized by their ability to inhibit the function of ATP synthase, an enzyme that plays a crucial role in energy production within cells. By binding to the F1 component of ATP synthase, oligomycins prevent the synthesis of ATP, which is a key source of energy for cellular processes.

These antibiotics have been used in research to study the mechanisms of ATP synthase and mitochondrial function. However, their therapeutic use as antibiotics is limited due to their toxicity to mammalian cells. Oligomycin A is one of the most well-known and studied members of this group of antibiotics.

Succinates, in a medical context, most commonly refer to the salts or esters of succinic acid. Succinic acid is a dicarboxylic acid that is involved in the Krebs cycle, which is a key metabolic pathway in cells that generates energy through the oxidation of acetyl-CoA derived from carbohydrates, fats, and proteins.

Succinates can also be used as a buffer in medical solutions and as a pharmaceutical intermediate in the synthesis of various drugs. In some cases, succinate may be used as a nutritional supplement or as a component of parenteral nutrition formulations to provide energy and help maintain acid-base balance in patients who are unable to eat normally.

It's worth noting that there is also a condition called "succinic semialdehyde dehydrogenase deficiency" which is a genetic disorder that affects the metabolism of the amino acid gamma-aminobutyric acid (GABA). This condition can lead to an accumulation of succinic semialdehyde and other metabolic byproducts, which can cause neurological symptoms such as developmental delay, hypotonia, and seizures.

Cytochromes are a type of hemeprotein found in the mitochondria and other cellular membranes of organisms. They contain a heme group, which is a prosthetic group composed of an iron atom surrounded by a porphyrin ring. This structure allows cytochromes to participate in redox reactions, acting as electron carriers in various biological processes.

There are several types of cytochromes, classified based on the type of heme they contain and their absorption spectra. Some of the most well-known cytochromes include:

* Cytochrome c: a small, mobile protein found in the inner mitochondrial membrane that plays a crucial role in the electron transport chain during cellular respiration.
* Cytochrome P450: a large family of enzymes involved in the metabolism of drugs, toxins, and other xenobiotics. They are found in various tissues, including the liver, lungs, and skin.
* Cytochrome b: a component of several electron transport chains, including those found in mitochondria, bacteria, and chloroplasts.

Cytochromes play essential roles in energy production, detoxification, and other metabolic processes, making them vital for the survival and function of living organisms.

Uncoupling agents are chemicals that interfere with the normal process of oxidative phosphorylation in cells. In this process, the energy from food is converted into ATP (adenosine triphosphate), which is the main source of energy for cellular functions. Uncouplers disrupt this process by preventing the transfer of high-energy electrons to oxygen, which normally drives the production of ATP.

Instead, the energy from these electrons is released as heat, leading to an increase in body temperature. This effect is similar to what happens during shivering or exercise, when the body generates heat to maintain its core temperature. Uncoupling agents are therefore also known as "mitochondrial protonophores" because they allow protons to leak across the inner mitochondrial membrane, bypassing the ATP synthase enzyme that would normally use the energy from this proton gradient to produce ATP.

Uncoupling agents have been studied for their potential therapeutic uses, such as in weight loss and the treatment of metabolic disorders. However, they can also be toxic at high doses, and their long-term effects on health are not well understood.

Quinone reductases are a group of enzymes that catalyze the reduction of quinones to hydroquinones, using NADH or NADPH as an electron donor. This reaction is important in the detoxification of quinones, which are potentially toxic compounds produced during the metabolism of certain drugs, chemicals, and endogenous substances.

There are two main types of quinone reductases: NQO1 (NAD(P)H:quinone oxidoreductase 1) and NQO2 (NAD(P)H:quinone oxidoreductase 2). NQO1 is a cytosolic enzyme that can reduce a wide range of quinones, while NQO2 is a mitochondrial enzyme with a narrower substrate specificity.

Quinone reductases have been studied for their potential role in cancer prevention and treatment, as they may help to protect cells from oxidative stress and DNA damage caused by quinones and other toxic compounds. Additionally, some quinone reductase inhibitors have been developed as chemotherapeutic agents, as they can enhance the cytotoxicity of certain drugs that require quinone reduction for activation.

Cytochrome b is a type of cytochrome, which is a class of proteins that contain heme as a cofactor and are involved in electron transfer. Cytochromes are classified based on the type of heme they contain and their absorption spectra.

The cytochrome b group includes several subfamilies of cytochromes, including cytochrome b5, cytochrome b2, and cytochrome bc1 (also known as complex III). These cytochromes are involved in various biological processes, such as fatty acid desaturation, steroid metabolism, and the electron transport chain.

The electron transport chain is a series of protein complexes in the inner mitochondrial membrane that generates most of the ATP (adenosine triphosphate) required for cellular energy production. Cytochrome bc1 is a key component of the electron transport chain, where it functions as a dimer and catalyzes the transfer of electrons from ubiquinol to cytochrome c while simultaneously pumping protons across the membrane. This creates an electrochemical gradient that drives ATP synthesis.

Deficiencies or mutations in cytochrome b genes can lead to various diseases, such as mitochondrial disorders and cancer.

Oxidation-Reduction (redox) reactions are a type of chemical reaction involving a transfer of electrons between two species. The substance that loses electrons in the reaction is oxidized, and the substance that gains electrons is reduced. Oxidation and reduction always occur together in a redox reaction, hence the term "oxidation-reduction."

In biological systems, redox reactions play a crucial role in many cellular processes, including energy production, metabolism, and signaling. The transfer of electrons in these reactions is often facilitated by specialized molecules called electron carriers, such as nicotinamide adenine dinucleotide (NAD+/NADH) and flavin adenine dinucleotide (FAD/FADH2).

The oxidation state of an element in a compound is a measure of the number of electrons that have been gained or lost relative to its neutral state. In redox reactions, the oxidation state of one or more elements changes as they gain or lose electrons. The substance that is oxidized has a higher oxidation state, while the substance that is reduced has a lower oxidation state.

Overall, oxidation-reduction reactions are fundamental to the functioning of living organisms and are involved in many important biological processes.

Amobarbital is a barbiturate drug that is primarily used as a sedative and sleep aid. It works by depressing the central nervous system, which can lead to relaxation, drowsiness, and reduced anxiety. Amobarbital is also sometimes used as an anticonvulsant to help control seizures.

Like other barbiturates, amobarbital has a high potential for abuse and addiction, and it can be dangerous or even fatal when taken in large doses or mixed with alcohol or other drugs. It is typically prescribed only for short-term use due to the risk of tolerance and dependence.

It's important to note that the use of barbiturates like amobarbital has declined in recent years due to the development of safer and more effective alternatives, such as benzodiazepines and non-benzodiazepine sleep aids.

Oxygen consumption, also known as oxygen uptake, is the amount of oxygen that is consumed or utilized by the body during a specific period of time, usually measured in liters per minute (L/min). It is a common measurement used in exercise physiology and critical care medicine to assess an individual's aerobic metabolism and overall health status.

In clinical settings, oxygen consumption is often measured during cardiopulmonary exercise testing (CPET) to evaluate cardiovascular function, pulmonary function, and exercise capacity in patients with various medical conditions such as heart failure, chronic obstructive pulmonary disease (COPD), and other respiratory or cardiac disorders.

During exercise, oxygen is consumed by the muscles to generate energy through a process called oxidative phosphorylation. The amount of oxygen consumed during exercise can provide important information about an individual's fitness level, exercise capacity, and overall health status. Additionally, measuring oxygen consumption can help healthcare providers assess the effectiveness of treatments and rehabilitation programs in patients with various medical conditions.

Succinic acid, also known as butanedioic acid, is an organic compound with the chemical formula HOOC(CH2)2COOH. It is a white crystalline powder that is soluble in water and has a slightly acerbic taste. In medicine, succinic acid is not used as a treatment for any specific condition. However, it is a naturally occurring substance found in the body and plays a role in the citric acid cycle, which is a key process in energy production within cells. It can also be found in some foods and is used in the manufacturing of various products such as pharmaceuticals, resins, and perfumes.

Potassium Cyanide (C6H5KN) is defined as a white, water-soluble, crystalline salt that is highly toxic. It is used in fumigation, electroplating, and metal cleaning. When combined with acids, it releases the deadly gas hydrogen cyanide. It can cause immediate death by inhibiting cellular respiration. It is also known as Cyanide of Potassium or Potassium Salt of Hydrocyanic Acid.

I'd be happy to help! However, I believe there might be a slight misunderstanding in your question. Mitochondria are organelles found in the cells of all complex living organisms, including humans, while the liver is a large, solid organ located in the upper right portion of the abdomen. They don't have a medical definition together. I can certainly provide you with separate definitions for each:

1. Mitochondria: These are double-membrane-bound cellular organelles that generate most of the chemical energy needed to power the cell's biochemical reactions. Commonly known as the "powerhouse of the cell," mitochondria convert organic substrates, such as glucose, fatty acids, and amino acids, into adenosine triphosphate (ATP) through a process called oxidative phosphorylation. Mitochondria are dynamic structures that can change their shape, size, and number through fission (division) and fusion (merging) processes. They play essential roles in various cellular functions, including calcium signaling, apoptosis (programmed cell death), and the regulation of cellular metabolism.

2. Liver: The liver is a large, lobulated organ that lies mainly in the upper right portion of the abdominal cavity, just below the diaphragm. It plays a crucial role in various physiological functions, such as detoxification, protein synthesis, metabolism, and nutrient storage. The liver is responsible for removing toxins from the bloodstream, producing bile to aid in digestion, regulating glucose levels, synthesizing plasma proteins, and storing glycogen, vitamins, and minerals. It also contributes to the metabolism of carbohydrates, lipids, and amino acids, helping maintain energy homeostasis in the body.

I hope this clarifies any confusion! If you have any further questions or need more information, please don't hesitate to ask.

Rhodobacter is not a medical term, but a genus of bacteria found in the environment. It is commonly found in aquatic environments and can perform photosynthesis, although it is not classified as a plant. Some species of Rhodobacter are capable of fixing nitrogen gas from the atmosphere, making them important contributors to the global nitrogen cycle.

While there may be some medical research into the potential uses or impacts of certain species of Rhodobacter, there is no widely recognized medical definition for this term. If you have any specific concerns about bacteria or infections, it's best to consult with a healthcare professional for accurate information and advice.

Carbonyl cyanide p-trifluoromethoxyphenylhydrazone (CCP) is a chemical compound that functions as an ionophore, which is a type of molecule that can transport ions across biological membranes. CCP is specifically known to transport protons (H+) and has been used in research as a tool to study the role of proton transport in various cellular processes.

CCP is also a potent mitochondrial uncoupler, which means that it disrupts the normal functioning of the mitochondria, the energy-producing structures in cells. By doing so, CCP can cause a rapid and irreversible decline in ATP (adenosine triphosphate) production, leading to cell death.

Due to its potent toxicity, CCP is not used as a therapeutic agent but rather as a research tool to study mitochondrial function and cellular metabolism. It is important to handle this compound with care and follow appropriate safety protocols when working with it in the laboratory.

Thenoyltrifluoroacetone (TTA) is not typically considered a medical compound, but rather a chemical compound with potential uses in various fields including chemistry, biology, and materials science. However, I can provide a general definition:

Thenoyltrifluoroacetone is an organofluorine compound with the formula C6H3F3O2S. It is a colorless liquid that is used as a fluorinated ligand in coordination chemistry and as a reagent in organic synthesis. Its unique chemical properties, such as its ability to act as a metal chelator and its volatility, have led to its use in various applications. Please consult relevant technical or scientific literature for more specific information regarding its uses and properties.

Cytochrome c1 is a protein that is a part of the electron transport chain in the inner mitochondrial membrane. It is a component of Complex III, also known as the cytochrome bc1 complex. Cytochrome c1 contains a heme group and plays a role in the transfer of electrons from ubiquinol to cytochrome c during oxidative phosphorylation, which is the process by which cells generate energy in the form of ATP. Defects in cytochrome c1 can lead to mitochondrial disorders and have been implicated in the development of certain diseases, such as neurodegenerative disorders and cancer.

Carbonyl cyanide m-chlorophenyl hydrazone (CCCP) is a chemical compound that is often used in research and scientific studies. It is an ionophore, which is a type of molecule that can transport ions across biological membranes. CCCP specifically transports protons (H+ ions) across membranes.

In biochemistry and cell biology, CCCP is commonly used as an uncoupler of oxidative phosphorylation. This is a process by which cells generate energy in the form of ATP (adenosine triphosphate) using the energy from the electron transport chain. By disrupting the proton gradient across the inner mitochondrial membrane, CCCP prevents the synthesis of ATP and causes a rapid depletion of cellular energy stores.

The medical relevance of CCCP is primarily limited to its use as a research tool in laboratory studies. It is not used as a therapeutic agent in clinical medicine.

Oxidoreductases are a class of enzymes that catalyze oxidation-reduction reactions, which involve the transfer of electrons from one molecule (the reductant) to another (the oxidant). These enzymes play a crucial role in various biological processes, including energy production, metabolism, and detoxification.

The oxidoreductase-catalyzed reaction typically involves the donation of electrons from a reducing agent (donor) to an oxidizing agent (acceptor), often through the transfer of hydrogen atoms or hydride ions. The enzyme itself does not undergo any permanent chemical change during this process, but rather acts as a catalyst to lower the activation energy required for the reaction to occur.

Oxidoreductases are classified and named based on the type of electron donor or acceptor involved in the reaction. For example, oxidoreductases that act on the CH-OH group of donors are called dehydrogenases, while those that act on the aldehyde or ketone groups are called oxidases. Other examples include reductases, peroxidases, and catalases.

Understanding the function and regulation of oxidoreductases is important for understanding various physiological processes and developing therapeutic strategies for diseases associated with impaired redox homeostasis, such as cancer, neurodegenerative disorders, and cardiovascular disease.

Ferricyanides are a class of chemical compounds that contain the ferricyanide ion (Fe(CN)6−3). The ferricyanide ion is composed of a central iron atom in the +3 oxidation state, surrounded by six cyanide ligands. Ferricyanides are strong oxidizing agents and are used in various chemical reactions, including analytical chemistry and as reagents in organic synthesis.

It's important to note that while ferricyanides themselves are not highly toxic, they can release cyanide ions if they are decomposed or reduced under certain conditions. Therefore, they should be handled with care and used in well-ventilated areas.

Dinitrophenols (DNP) are a class of chemical compounds that contain two nitro groups (-NO2) attached to a phenol group. Dinitrophenols have been used in the past as industrial dyes, wood preservatives, and pesticides. However, they have also been misused as weight loss supplements due to their ability to increase metabolic rate and cause weight loss.

The use of DNP for weight loss is dangerous and has been linked to several fatalities. DNP works by disrupting the normal functioning of the mitochondria in cells, which are responsible for producing energy. This disruption causes an increase in metabolic rate, leading to a rapid breakdown of fat and carbohydrates, and ultimately weight loss. However, this increased metabolism can also produce excessive heat, leading to hyperthermia, dehydration, and damage to organs such as the heart, liver, and kidneys.

Due to their potential for serious harm, DNP-containing products are banned in many countries, including the United States. Medical professionals should be aware of the dangers associated with DNP use and advise patients accordingly.

Thiazoles are organic compounds that contain a heterocyclic ring consisting of a nitrogen atom and a sulfur atom, along with two carbon atoms and two hydrogen atoms. They have the chemical formula C3H4NS. Thiazoles are present in various natural and synthetic substances, including some vitamins, drugs, and dyes. In the context of medicine, thiazole derivatives have been developed as pharmaceuticals for their diverse biological activities, such as anti-inflammatory, antifungal, antibacterial, and antihypertensive properties. Some well-known examples include thiazide diuretics (e.g., hydrochlorothiazide) used to treat high blood pressure and edema, and the antidiabetic drug pioglitazone.

Dimercaprol is a chelating agent, which means it can bind to and help remove certain toxic substances from the body. It is primarily used in the treatment of heavy metal poisoning, such as lead, mercury, or arsenic poisoning. Dimercaprol works by forming stable complexes with these toxic metals, allowing them to be excreted from the body through urine and bile.

The chemical name for dimercaprol is British Anti-Lewisite (BAL), as it was initially developed during World War II as an antidote against the chemical warfare agent Lewisite, a type of arsenic-based blistering agent. Dimercaprol is administered parenterally, usually by intramuscular injection, and its use requires medical supervision due to potential side effects, including hypertension, tachycardia, nausea, vomiting, and pain at the injection site.

Submitochondrial particles, also known as "submitochondrial vesicles" or "inner membrane fragments," are small particles that consist of the inner mitochondrial membrane and the associated components. They are obtained through sonication or other methods of disrupting mitochondria, which results in breaking down the outer membrane while leaving the inner membrane intact. These particles can be used in various biochemical studies to investigate the structure, function, and composition of the inner mitochondrial membrane and its components, such as the electron transport chain and ATP synthase complexes.

NADH dehydrogenase, also known as Complex I, is an enzyme complex in the electron transport chain located in the inner mitochondrial membrane. It catalyzes the oxidation of NADH to NAD+ and the reduction of coenzyme Q to ubiquinol, playing a crucial role in cellular respiration and energy production. The reaction involves the transfer of electrons from NADH to coenzyme Q, which contributes to the generation of a proton gradient across the membrane, ultimately leading to ATP synthesis. Defects in NADH dehydrogenase can result in various mitochondrial diseases and disorders.

Reactive Oxygen Species (ROS) are highly reactive molecules containing oxygen, including peroxides, superoxide, hydroxyl radical, and singlet oxygen. They are naturally produced as byproducts of normal cellular metabolism in the mitochondria, and can also be generated by external sources such as ionizing radiation, tobacco smoke, and air pollutants. At low or moderate concentrations, ROS play important roles in cell signaling and homeostasis, but at high concentrations, they can cause significant damage to cell structures, including lipids, proteins, and DNA, leading to oxidative stress and potential cell death.

I'm happy to help! However, it seems like there are two terms combined into one request: "Mitochondria" and "Heart." I will provide separate definitions for each.

Mitochondrion (singular) or Mitochondria (plural): These are specialized structures found in the cytoplasm of most eukaryotic cells (cells with a true nucleus), including human cells. They are often referred to as the "powerhouse" of the cell because they generate energy in the form of ATP (adenosine triphosphate) through a process called oxidative phosphorylation. Mitochondria contain their own DNA, which is distinct from the nuclear DNA, and are believed to have originated from ancient bacteria that established a symbiotic relationship with primitive eukaryotic cells.

Heart: In human anatomy, the heart is a muscular organ responsible for pumping blood throughout the body. It is located in the thoracic cavity, slightly left of the center, and is enclosed by the pericardium, a double-walled sac that provides protection and lubrication for the heart's movement. The human heart is divided into four chambers: two atria on the top and two ventricles on the bottom. The right side of the heart receives deoxygenated blood from the body and pumps it to the lungs, while the left side receives oxygenated blood from the lungs and pumps it to the rest of the body. The heart's pumping action is regulated by electrical signals that originate in a group of specialized cardiac muscle cells called the sinoatrial node (SA node).

Cell respiration is the process by which cells convert biochemical energy from nutrients into adenosine triphosphate (ATP), and then release waste products. The three main stages of cell respiration are glycolysis, the citric acid cycle (also known as the Krebs cycle), and the electron transport chain.

During glycolysis, which takes place in the cytoplasm, glucose is broken down into two molecules of pyruvate, producing a small amount of ATP and reducing power in the form of NADH.

The citric acid cycle occurs in the mitochondria and involves the breakdown of acetyl-CoA (formed from pyruvate) to produce more ATP, NADH, and FADH2.

Finally, the electron transport chain, also located in the mitochondria, uses the energy from NADH and FADH2 to pump protons across the inner mitochondrial membrane, creating a proton gradient. The flow of protons back across the membrane drives the synthesis of ATP, which is used as a source of energy by the cell.

Cell respiration is a crucial process that allows cells to generate the energy they need to perform various functions and maintain homeostasis.

Oxidative phosphorylation is the metabolic process by which cells use enzymes to generate energy in the form of adenosine triphosphate (ATP) from the oxidation of nutrients, such as glucose or fatty acids. This process occurs in the inner mitochondrial membrane of eukaryotic cells and is facilitated by the electron transport chain, which consists of a series of protein complexes that transfer electrons from donor molecules to acceptor molecules. As the electrons are passed along the chain, they release energy that is used to pump protons across the membrane, creating a gradient. The ATP synthase enzyme then uses the flow of protons back across the membrane to generate ATP, which serves as the main energy currency for cellular processes.

Adenosine Triphosphate (ATP) is a high-energy molecule that stores and transports energy within cells. It is the main source of energy for most cellular processes, including muscle contraction, nerve impulse transmission, and protein synthesis. ATP is composed of a base (adenine), a sugar (ribose), and three phosphate groups. The bonds between these phosphate groups contain a significant amount of energy, which can be released when the bond between the second and third phosphate group is broken, resulting in the formation of adenosine diphosphate (ADP) and inorganic phosphate. This process is known as hydrolysis and can be catalyzed by various enzymes to drive a wide range of cellular functions. ATP can also be regenerated from ADP through various metabolic pathways, such as oxidative phosphorylation or substrate-level phosphorylation, allowing for the continuous supply of energy to cells.

Diuron is a pesticide and herbicide that is used to control weeds in various settings, such as agriculture, landscaping, and forestry. Its chemical name is 3-(3,4-dichlorophenyl)-1,1-dimethylurea. Diuron works by inhibiting photosynthesis in plants, which prevents them from growing and eventually kills them.

While diuron is effective at controlling weeds, it can also have harmful effects on non-target organisms, including aquatic life and pollinators. Additionally, there are concerns about the potential for diuron to contaminate water sources and pose risks to human health. As a result, its use is regulated in many countries, and there are restrictions on how it can be applied and disposed of.

It's worth noting that Diuron is not a medical term or a drug used for treating any medical condition in humans or animals.

Spectrophotometry is a technical analytical method used in the field of medicine and science to measure the amount of light absorbed or transmitted by a substance at specific wavelengths. This technique involves the use of a spectrophotometer, an instrument that measures the intensity of light as it passes through a sample.

In medical applications, spectrophotometry is often used in laboratory settings to analyze various biological samples such as blood, urine, and tissues. For example, it can be used to measure the concentration of specific chemicals or compounds in a sample by measuring the amount of light that is absorbed or transmitted at specific wavelengths.

In addition, spectrophotometry can also be used to assess the properties of biological tissues, such as their optical density and thickness. This information can be useful in the diagnosis and treatment of various medical conditions, including skin disorders, eye diseases, and cancer.

Overall, spectrophotometry is a valuable tool for medical professionals and researchers seeking to understand the composition and properties of various biological samples and tissues.

NAD (Nicotinamide Adenine Dinucleotide) is a coenzyme found in all living cells. It plays an essential role in cellular metabolism, particularly in redox reactions, where it acts as an electron carrier. NAD exists in two forms: NAD+, which accepts electrons and becomes reduced to NADH. This pairing of NAD+/NADH is involved in many fundamental biological processes such as generating energy in the form of ATP during cellular respiration, and serving as a critical cofactor for various enzymes that regulate cellular functions like DNA repair, gene expression, and cell death.

Maintaining optimal levels of NAD+/NADH is crucial for overall health and longevity, as it declines with age and in certain disease states. Therefore, strategies to boost NAD+ levels are being actively researched for their potential therapeutic benefits in various conditions such as aging, neurodegenerative disorders, and metabolic diseases.

Antimetabolites are a class of drugs that interfere with the normal metabolic processes of cells, particularly those involved in DNA replication and cell division. They are commonly used as chemotherapeutic agents to treat various types of cancer because many cancer cells divide more rapidly than normal cells. Antimetabolites work by mimicking natural substances needed for cell growth and division, such as nucleotides or amino acids, and getting incorporated into the growing cells' DNA or protein structures, which ultimately leads to the termination of cell division and death of the cancer cells. Examples of antimetabolites include methotrexate, 5-fluorouracil, and capecitabine.

Cytochrome c is a small protein that is involved in the electron transport chain, a key part of cellular respiration in which cells generate energy in the form of ATP. Cytochrome c contains a heme group, which binds to and transports electrons. The cytochrome c group refers to a class of related cytochromes that have similar structures and functions. These proteins are found in the mitochondria of eukaryotic cells (such as those of plants and animals) and in the inner membranes of bacteria. They play a crucial role in the production of energy within the cell, and are also involved in certain types of programmed cell death (apoptosis).

NADH, NADPH oxidoreductases are a class of enzymes that catalyze the redox reaction between NADH or NADPH and various electron acceptors. These enzymes play a crucial role in cellular metabolism by transferring electrons from NADH or NADPH to other molecules, which is essential for many biochemical reactions.

NADH (nicotinamide adenine dinucleotide hydrogen) and NADPH (nicotinamide adenine dinucleotide phosphate hydrogen) are coenzymes that act as electron carriers in redox reactions. They consist of a nicotinamide ring, which undergoes reduction or oxidation by accepting or donating electrons and a proton (H+).

NADH, NADPH oxidoreductases are classified based on their structure and mechanism of action. Some examples include:

1. Dehydrogenases: These enzymes catalyze the oxidation of NADH or NADPH to NAD+ or NADP+ while reducing an organic substrate. Examples include lactate dehydrogenase, alcohol dehydrogenase, and malate dehydrogenase.
2. Oxidases: These enzymes catalyze the oxidation of NADH or NADPH to NAD+ or NADP+ while reducing molecular oxygen (O2) to water (H2O). Examples include NADH oxidase and NADPH oxidase.
3. Reductases: These enzymes catalyze the reduction of various electron acceptors using NADH or NADPH as a source of electrons. Examples include glutathione reductase, thioredoxin reductase, and nitrate reductase.

Overall, NADH, NADPH oxidoreductases are essential for maintaining the redox balance in cells and play a critical role in various metabolic pathways, including energy production, detoxification, and biosynthesis.

Salicylamides are organic compounds that consist of a salicylic acid molecule (a type of phenolic acid) linked to an amide group. They are derivatives of salicylic acid and are known for their analgesic, anti-inflammatory, and antipyretic properties. Salicylamides have been used in various pharmaceutical and therapeutic applications, including the treatment of pain, fever, and inflammation. However, they have largely been replaced by other compounds such as acetylsalicylic acid (aspirin) due to their lower potency and potential side effects.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

Hydrogen peroxide (H2O2) is a colorless, odorless, clear liquid with a slightly sweet taste, although drinking it is harmful and can cause poisoning. It is a weak oxidizing agent and is used as an antiseptic and a bleaching agent. In diluted form, it is used to disinfect wounds and kill bacteria and viruses on the skin; in higher concentrations, it can be used to bleach hair or remove stains from clothing. It is also used as a propellant in rocketry and in certain industrial processes. Chemically, hydrogen peroxide is composed of two hydrogen atoms and two oxygen atoms, and it is structurally similar to water (H2O), with an extra oxygen atom. This gives it its oxidizing properties, as the additional oxygen can be released and used to react with other substances.

Ferrocyanides are salts or complex ions containing the ferrocyanide ion (Fe(CN)2-4). The ferrocyanide ion is a stable, soluble, and brightly colored complex that contains iron in the +2 oxidation state coordinated to four cyanide ligands. Ferrocyanides are commonly used in various industrial applications such as water treatment, chemical synthesis, and photography due to their stability and reactivity. However, they can be toxic if ingested or inhaled in large quantities, so proper handling and disposal procedures should be followed.

Cytochromes b are a group of electron transport proteins that contain a heme c group, which is the prosthetic group responsible for their redox activity. They play a crucial role in the electron transport chain (ETC) located in the inner mitochondrial membrane of eukaryotic cells and in the plasma membrane of prokaryotic cells.

The cytochromes b are part of Complex III, also known as the cytochrome bc1 complex or ubiquinol-cytochrome c reductase, in the ETC. In this complex, they function as electron carriers between ubiquinone (Q) and cytochrome c, participating in the process of oxidative phosphorylation to generate ATP.

There are multiple isoforms of cytochromes b found in various organisms, with different numbers of subunits and structures. However, they all share a common function as essential components of the electron transport chain, facilitating the transfer of electrons during cellular respiration and energy production.

... A Urauchimycin Seipke, Ryan F; Hutchings, Matthew I (2013). "The regulation and biosynthesis of antimycins". ... Antimycins are produced by a non-ribosomal peptide synthetase (NRPS)/polyketide synthase (PKS) assembly complex which acts as ... Antimycins are produced as secondary metabolites by Streptomyces bacteria, a soil bacteria. These specialized metabolites ... The following steps describe chemically what the Ant Enzymes do in order to synthesize Antimycin. Synthesis begins with ...
When Antimycin A is added at 25 ppb it provides a complete kill. However at 10 ppb, Antimycin A is used as a selective killing ... Antimycin A (more exactly Antimycin A1b) is a secondary metabolite produced by Streptomyces bacteria and a member of a group of ... Antimycin A is an inhibitor of cellular respiration, specifically oxidative phosphorylation. Antimycin A binds to the Qi site ... March 2001) "Material Safety Data Sheet - Antimycin A" (PDF). Santa Cruz Biotechnology. "Antimycin A". TOXNET. National ...
... s are antimycin antibiotics isolated from marine actinomycete. Imamura, N.; Nishijima, M.; Adachi, K.; Sano, H. ( ... 1993). "Novel antimycin antibiotics, urauchimycins a and B, produced by marine actinomycete". The Journal of Antibiotics. 46 (2 ...
"Two Antimycin A Analogues from Marine-Derived Actinomycete Streptomyces lusitanus". Marine Drugs. 10 (12): 668-676. doi:10.3390 ...
Examples of piscicides include rotenone, saponins, TFM, niclosamide and Antimycin A (Fintrol). Historically, fishing techniques ...
This complex is inhibited by dimercaprol (British Antilewisite, BAL), naphthoquinone and antimycin. In Complex IV (cytochrome c ... by a high membrane potential or respiratory inhibitors such as antimycin A), Complex III may leak electrons to molecular oxygen ...
When piscides are used, antimycin is often the preferred choice as there is little impact on lake invertebrates and its ... Two of the traditionally used piscidies in lake management are rotenone and antimycin. Chemical applications are often looked ...
As such, standard fish poisons or piscicides (e.g., rotenone and antimycin A) that are transmitted across the gill membrane may ... Serial pesticide dilutions of antimycin-A were tested and found to be innocuous. No changes in morbidity and mortality were ...
Reconstitution of antimycin-insensitive electron transfer with the iron-sulfur protein and cytochrome c1". The Journal of ...
Tappel had the (erroneous) idea that inhibitors like antimycin and alkyl hydroxyquinoline-N-oxide might work by chelating iron ... "Inhibition of electron transport by antimycin A, alkyl hydroxy naphthoquinones and metal coordination compounds". Biochem. ...
Reconstitution of antimycin-insensitive electron transfer with the iron-sulfur protein and cytochrome c1". The Journal of ...
The fungus is also susceptible to antimycins produced by Streptomyces species. Conversely, P. fastigiata exhibits antimicrobial ...
"Complete Inhibition of Electron Transfer from Ubiquinol to Cytochrome by the Combined Action of Antimycin and Myxothiazol". ...
Smith MJ, Simco BA, Warren CO (December 1975). "Comparative effects of antimycin A on isolated mitochondria of channel catfish ...
... except when inhibited by antimycin A". Journal of Neurochemistry. 148 (6): 731-745. doi:10.1111/jnc.14654. PMC 7086484. PMID ...
Electron leakage occurs mainly at the Qo site and is stimulated by antimycin A. Antimycin A locks the b hemes in the reduced ... Antimycin A binds to the Qi site and inhibits the transfer of electrons in Complex III from heme bH to oxidized Q (Qi site ...
An antibiotic, antimycin A, and British anti-Lewisite, an antidote used against chemical weapons, are the two important ...
There are other chemicals that interrupt the mitochondrial electron transport chain (e.g., rotenone, antimycin A) and produce ...
Oxygen, O2 Ozonide, O− 3 Peroxide, O2− 2 Oxide, O2− Dioxygenyl, O+ 2 Antimycin A - used in fishery management, this compound ...
This can be done by poisoning rivers with chemicals such as antimycin or rotenone which have been declared safe in the U.S. by ...
SirexAA-E. Antimycin A - Chemical compound produced by Stroptomyces used as a piscicide Geosmin - Chemical compound responsible ...
... and introduction of the toxin and inhibitor of cellular respiration antimycin A. They also created small barriers to keep new ...
... antimycin a MeSH D02.540.505.100 - brefeldin a MeSH D02.540.505.125 - candicidin MeSH D02.540.505.187 - epothilones MeSH ...
... is used in biomedical research to study the oxygen consumption rate of cells, usually in combination with antimycin A ...
He showed that the binding of certain inhibitors of oxidative phosphorylation acting at different sites (antimycin on electron ...
Antimony pentafluoride Antimycin A ANTU (Alpha-Naphthylthiourea) Arsenic pentoxide Arsenous oxide Arsenous trichloride Arsine ...
... antimycin a MeSH D04.345.349.100 - brefeldin a MeSH D04.345.349.125 - candicidin MeSH D04.345.349.156 - cytochalasins MeSH ...
Antimycin A Urauchimycin Seipke, Ryan F; Hutchings, Matthew I (2013). "The regulation and biosynthesis of antimycins". ... Antimycins are produced by a non-ribosomal peptide synthetase (NRPS)/polyketide synthase (PKS) assembly complex which acts as ... Antimycins are produced as secondary metabolites by Streptomyces bacteria, a soil bacteria. These specialized metabolites ... The following steps describe chemically what the Ant Enzymes do in order to synthesize Antimycin. Synthesis begins with ...
Parkin-mediated ubiquitylation redistributes MITOL/March5 from mitochondria to peroxisomes. by Fumika Koyano, Koji Yamano, Hidetaka Kosako, Yoko Kimura, Mayumi Kimura, Yukio Fujiki, Keiji Tanaka, Noriyuki Matsuda. EMBO reports. Read more related scholarly scientific articles and abstracts.
Oligo, oligomycin; CCCP, carbonyl cyanide m-chlorophenyl hydrazine; Ant A, antimycin A. Data are represented as mean ± SEM ... 2N, diploid; 4N, tetraploid; Oligo, Oligomycin; CCCP, Carbonyl cyanide m-chlorophenyl hydrazine; Ant A, Antimycin A. The ... and 5 µM Antimycin A was added to inhibit complex III. For respiration measurements in immortalized spermatocytes (GC2spd(ts ...
... for antimycin A (lilac). Values are medians with 95% CI, representing error; Kruskal-Wallis test H = 38.96, n1 = 28, n2 = 31, n ... using rotenone and antimycin A, which are complex I and III inhibitors, respectively. After 24 h, we recorded an ∼30% increase ... and the complex III inhibitor antimycin A (1 µm AA). Redox ratios are normalized to control (DMSO/vehicle, CTRL) values at the ... rotenone/antimycin A [AA]). Mitochondrial trafficking and fusion in axons were quantified by using the Just Another ...
The data were then validated by injection of oligomycin (18.5 µM), rotenone/antimycin A (6.6 µM), and carbonyl cyanide m- ...
The use of other myocardial perfusion agents, as in indium-111 antimycin scintigraphy, has shown the potential of this modality ...
... antimycin-A were 1 μM each and were prepared in the XF Assay media in order to assess for ATP-dependent, maximal, and ... and 1 μm rotenone/antimycin A to determine the ATP-linked OCRs, maximal OCRs, and mitochondrially-derived OCRs, respectively, ...
Y. H. Han and W. H. Park, "Growth inhibition in antimycin a treated-lung cancer Calu-6 cells via inducing a G1 phase arrest and ...
Succinate respiration was sensitive to myxothiazol, antimycin A and 2-heptyl-4-hydroxyquinoline-N-oxide (HQNO). Juglone, ... Succinate respiration was sensitive to myxothiazol, antimycin A and 2-heptyl-4-hydroxyquinoline-N-oxide (HQNO). Juglone, ...
AA: antimycin A; ECAR: extracellular acidification rate; F: carbonyl cyanide-p-trifluoromethoxyphenylhydrazone (FCCP); MMP: ... AA: antimycin A; ECAR: extracellular acidification rate; F: carbonyl cyanide-p-trifluoromethoxyphenylhydrazone (FCCP); MMP: ... Minimum rate measurement after rotenone/antimycin A injection. 1g. Basal Respiration. (Last rate measurement before first ... and a combination of antimycin A (0.5 µM) and rotenone (1 µM). The obtained data were analyzed on the Agilent Seahorse ...
... antimycin A 1 µg/mL (ANTI), complex III inhibitor; oligomycin 5 µM (OLIGO), ATP synthase inhibitor, and 0.5% DMSO, vehicle (CTR ...
Injection of 200?nM antimycin shows similar non\mitochondrial respiration rates for both Stat3+/+ and Stat3?/? cells. Mean and ... nM antimycin were injected and resulted in a higher mitochondrial respiration NU2058 activity in cells cultured in the presence ...
2 µM oligomycin, 2 µM FCCP and 2 µM antimycin A were injected consecutively during the measurement. (D) Basal OCR and ECAR ... 2 µM oligomycin, 2 µM FCCP and 2 µM antimycin A were injected consecutively during the measurement. (I) Basal OCR and ECAR ... 2 µM oligomycin, 2 µM FCCP, and 2 µM antimycin A were injected consecutively during the measurement. C Bioenergetic parameters ... 2 µM oligomycin, 2 µM FCCP and 2 µM antimycin A were injected consecutively during the measurement. (E) Bioenergetic parameters ...
MOLECULAR DOCKING STUDIES OF OPENED-CHAIN ANALOGUES OF ANTIMYCIN A ASCASPASES INHIBITORS OF APOPTOSIS IN COLORECTAL CANCER 3 ...
Anti-mycin A, a complex III inhibitor known to generate reactive oxygen species, decreased INa. This effect was blocked by NAD ...
Antimycin A is an antibiotic substance produced by various species of Streptomyces bacteria. It is known to inhibit the ... Antimycin A is a antibiotic compound derived from various Streptomyces bacteria species, acting as an electron transport chain ... In a medical context, antimycin A is not used as a therapeutic agent due to its toxicity to mammalian cells. However, it may be ... Antimycin A has been used in research to study the mechanisms of cellular respiration and oxidative phosphorylation. ...
Biphasic oxygen kinetics of cellular respiration and linear oxygen dependence of antimycin A inhibited oxygen consumption. Mol ...
... and 1.8 M antimycin A. Mitochondrial Ca2+ uptake was estimated fluorimetrically with Fura-6F (340/380 nm excitation and 510 nm ...
Antimycin A D2.540.505.75 D2.540.576.500.750 Antirrhinum B1.650.940.800.575.100.892.55 B1.650.940.800.575.100.583.700.67 ...
D1.632.80 Antimycin A D4.345.349.75 Appendicitis C1.539.463.99 Argon Plasma Coagulation E2.520.425.500 E2.154.402.54 E2.520. ...
Title : Poliomyelitis in Idaho after use of live virus vaccine Personal Author(s) : Eklund, Carl M.;Bell, E. John;Gerloff, Robert K.;LaVeck. Gerald D.;Silverman, Gerald M.;Sunada, Kayo;Hopkey, Ione; Published Date : Jul 1958 Source : Public Health Rep. 73(7):637-647 URL : https://stacks.cdc.gov/view/cdc/73024 ...
Antimycin A1. Change simulation parameters The result was obtained by a proprietary SIELC algorithm. It may deviate from the ... Antimycin A1. *(2R,3S,6S,7R,8R)-3-(3-Formamido-2-hydroxybenzamido)-8-hexyl-2,6-dimethyl-4,9-dioxo-1,5-dioxonan-7-yl 3- ... Antimycin A1 can be analyzed by this reverse phase (RP) HPLC method with simple conditions. The mobile phase contains an ... Separation of Antimycin A1 on Newcrom R1 HPLC column. February 16, 2018. ...
antimycin. After the Seahorse analysis, cells were fixed in 4% paraformaldehyde for 30 min and stained with Janus Green. ...
... or antimycin. Antimycin binds to cytochrome c reductase and leads to the formation of large quantities of ROS (27). As shown in ... We observed this effect of H2O2, paraquat, and antimycin on ERK phosphorylation in both AMPKα+/+ and AMPKα−/− cell lines. In ... Metformin blocks paraquat-induced and antimycin-induced, but not H2O2-induced, ERK activation. ROS increases ERK signaling (26 ... 1E, treatment with paraquat or antimycin for 30 minutes led to a marked increase in p-ERK, consistent with increases in ROS. ...
Antimycin A (which inhibits electron transfer and, hence, OXPHOS) served as a positive control. In the absence of LRP130, fatty ...
PDB Description: stigmatellin and antimycin bound cytochrome bc1 complex from chicken. PDB Compounds: (H:) ubiquinol cytochrome ...
MeSH Terms: Antimycin A/toxicity; Ataxia Telangiectasia Mutated Proteins/metabolism*; Cell Hypoxia*; Cell Line, Tumor; DNA ... ATM was not required for activating p53 when mitochondrial respiration was inhibited by chronic exposure to antimycin A. Also, ...
mTORC1 activity was assayed in response to a 6-h treatment with vehicle (DMSO), piericidin (500 nM), antimycin (500 nM), or ... antimycin, or oligomycin. (E) Model for pathway leading to mTORC1 inhibition in response to mitochondrial distress. ... induced by the ATP synthase inhibitor oligomycin as well as the electron transport chain inhibitors piericidin and antimycin. ...
A/R, antimycin plus rotenone. Measures of mitochondrial function (defined in Supplementary Fig. 5b,c) were quantitatively ...
... the effects of impairment of mitochondrial function and activity on myogenic cells have been investigated using antimycin [24 ... as shown in other mitochondrial inhibitors including antimycin, azide, CCCP, and valinomycin [24]. Therefore, increased ...
An ROS generator, antimycin A, inhibits the growth of HeLa cells via apoptosis.. Park WH; Han YW; Kim SH; Kim SZ. J Cell ... Growth inhibition in antimycin A treated-lung cancer Calu-6 cells via inducing a G1 phase arrest and apoptosis.. Han YH; Park ... Antimycin A as a mitochondrial electron transport inhibitor prevents the growth of human lung cancer A549 cells.. Han YH; Kim ... 2. The effects of antimycin A on endothelial cells in cell death, reactive oxygen species and GSH levels.. You BR; Park WH. ...
... and antimycin A were injected through the ports of the Seahorse Flux Pak cartridge to reach final concentrations of 1 μg/mL, ...
C1 1397-94-0 Antimycin A DTXSID9032325 - - - 741-58-2 Bensulide DTXSID9032329 CC(C)OP(=S)(OC(C)C)SCCNS(=O)(=O)C1=CC=CC=C1 ...
D1.632.80 Antimycin A D4.345.349.75 Appendicitis C1.539.463.99 Argon Plasma Coagulation E2.520.425.500 E2.154.402.54 E2.520. ...
Antimycin A1 Narrower Concept UI. M0001480. Registry Number. 0. Terms. Antimycin A1 Preferred Term Term UI T002976. Date09/18/ ... Antimycin A1 has been used as a fungicide, insecticide, and miticide. (From Merck Index, 12th ed). Terms. Antimycin A Preferred ... Antimycin A1 has been used as a fungicide, insecticide, and miticide. (From Merck Index, 12th ed). Entry Term(s). Antimycin A1 ... Antimycin A Preferred Concept UI. M0001479. Registry Number. 642-15-9. Scope Note. An antibiotic substance produced by ...
Antimycin A1 Narrower Concept UI. M0001480. Registry Number. 0. Terms. Antimycin A1 Preferred Term Term UI T002976. Date09/18/ ... Antimycin A1 has been used as a fungicide, insecticide, and miticide. (From Merck Index, 12th ed). Terms. Antimycin A Preferred ... Antimycin A1 has been used as a fungicide, insecticide, and miticide. (From Merck Index, 12th ed). Entry Term(s). Antimycin A1 ... Antimycin A Preferred Concept UI. M0001479. Registry Number. 642-15-9. Scope Note. An antibiotic substance produced by ...
... oxidized cytochrome c as acceptor and antimycin-A as the complex III specific inhibitor. The reduction of cytochrome c as ...
Antimycin A - Preferred Concept UI. M0001479. Scope note. An antibiotic substance produced by Streptomyces species. It inhibits ... Antimycin A1 has been used as a fungicide, insecticide, and miticide. (From Merck Index, 12th ed) ... Antimycin A1 has been used as a fungicide, insecticide, and miticide. (From Merck Index, 12th ed). ...
Antimycin A (50 muM) caused a time-dependent, irreversible decrease in adenine nucleotides. ... Effects of an electron transport inhibitor (antimycin A) on mucosal nucleotides was determined in a whole tissue model. In the ... Effects of an electron transport inhibitor (antimycin A) on mucosal nucleotides was determined in a whole tissue model. In the ... Antimycin A (50 muM) caused a time-dependent, irreversible decrease in adenine nucleotides. ...
Respiratory inhibitors, oligomycin, FCCP (uncoupling agent), and rotenone/antimycin A were used to measure basal oxygen ...
This contraction is blocked by antimycin A and/or oligomycin. Hence, the ATP which causes myofibrillar contraction is produced ... Myofibrillar contraction is unaffected by the presence of antimycin A or oligomycin. However, myofibrils in the presence of ... hydrolysis of ATP since it is blocked by either antimycin A or oligomycin. The other assay tested for the production of ATP ...
N0000166272 Antimony N0000006951 Antimony Potassium Tartrate N0000168480 Antimony Sodium Gluconate N0000167393 Antimycin A ...
It was inhibited by antimycin A, dicumarol, and o-iodosobenzoic acid; and it was inactivated by ammonium sulfate precipitation ...
Final compound concentrations were 2 μM oligomycin, 1 μM FCCP, and 1 μM/2 μM rotenone/antimycin A. For the permeabilization ...
  • Antimycins are produced as secondary metabolites by Streptomyces bacteria, a soil bacteria. (wikipedia.org)
  • Antimycin A from Streptomyces sp. (sigmaaldrich.com)
  • The dependence of brain mitochondria reactive oxygen species production on oxygen level is linear, except when inhibited by antimycin A. . J Neurochem. (cornell.edu)
  • Hütter E, Renner K, Jansen-Dürr P, Gnaiger E (2002) Biphasic oxygen kinetics of cellular respiration and linear oxygen dependence of antimycin A inhibited oxygen consumption. (bioblast.at)
  • Antimycins are produced by a non-ribosomal peptide synthetase (NRPS)/polyketide synthase (PKS) assembly complex which acts as an assembly line for antimycin production. (wikipedia.org)
  • 13. Antimycin A as a mitochondrial electron transport inhibitor prevents the growth of human lung cancer A549 cells. (nih.gov)
  • Effects of an electron transport inhibitor (antimycin A) on mucosal nucleotides was determined in a whole tissue model. (lsu.edu)
  • Respiratory inhibitors, oligomycin, FCCP (uncoupling agent), and rotenone/antimycin A were used to measure basal oxygen consumption rate, maximal/spare respiration, as well as extracellular acidification rate from peripheral blood mononuclear cells (PBMC) collected from a healthy control. (nih.gov)
  • We have therefore investigated the effects of rotenone, myxothiazol, antimycin A, cyanide (CN(-)) and oligomycin on isolated carotid body type I cells. (ox.ac.uk)
  • Current approaches to initiate mitophagy include acute dissipation of the mitochondrial membrane potential (ΔΨm) by mitochondrial uncouplers (for example, FCCP/CCCP) and the use of antimycin A and oligomycin to impair respiration. (core.ac.uk)
  • ATM was not required for activating p53 when mitochondrial respiration was inhibited by chronic exposure to antimycin A. Also, ATM was not further activated by mitochondrial ROS, which were enhanced by depleting manganese superoxide dismutase (SOD2). (nih.gov)
  • 10. Growth inhibition in antimycin A treated-lung cancer Calu-6 cells via inducing a G1 phase arrest and apoptosis. (nih.gov)
  • 11. An ROS generator, antimycin A, inhibits the growth of HeLa cells via apoptosis. (nih.gov)
  • Passage control and SWCNT-transformed human lung epithelial cells were treated with known inducers of apoptosis via the intrinsic (antimycin A and CDDP) or extrinsic (FasL and TNF-a) pathway and analyzed for apoptosis by DNA fragmentation, annexin-V expression, and caspase activation assays. (cdc.gov)
  • 1. The effects of N-acetyl cysteine, buthionine sulfoximine, diethyldithiocarbamate or 3-amino-1,2,4-triazole on antimycin A-treated Calu-6 lung cells in relation to cell growth, reactive oxygen species and glutathione. (nih.gov)
  • 2. The effects of antimycin A on endothelial cells in cell death, reactive oxygen species and GSH levels. (nih.gov)
  • 9. Tiron, a ROS scavenger, protects human lung cancer Calu-6 cells against antimycin A-induced cell death. (nih.gov)