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Oligomycin
Oligomycin
Oligomycin
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Oligomycin A
Names
IUPAC name
(1R,4E,5'S,6S,6'S,7R,8S,10R,11R,12S,14R,15S,16R,18E,20E,22R,25S,27R,28S,29R)-22-ethyl-7,11,14,15-tetrahydroxy-6'-[(2R)-2-hydroxypropyl]-5',6,8,10,12,14,16,28,29-nonamethyl-3',4',5',6'-tetrahydro-3H,9H,13H-spiro[2,26-dioxabicyclo[23.3.1]nonacosa-4,18,20-triene-27,2'-pyran]-3,9,13-trione
Other names
Oligomycin
Identifiers
3D model (JSmol)
ChEBI
ChemSpider
ECHA InfoCard 100.014.334 Edit this at Wikidata
EC Number
  • 215-767-9
MeSH Oligomycins
RTECS number
  • RK3325000
UNII
  • InChI=1S/C46H76O11/c1-13-34-18-16-14-15-17-28(4)42(51)45(12,54)43(52)32(8)40(50)31(7)39(49)30(6)38(48)27(3)19-22-37(47)55-41-29(5)35(21-20-34)56-46(33(41)9)24-23-26(2)36(57-46)25-44(10,11)53/h14-16,18-19,22,26-36,38,40-42,48,50-51,53-54H,13,17,20-21,23-25H2,1-12H3/b15-14+,18-16-,22-19+/t26-,27-,28+,29+,30+,31-,32-,33-,34+,35?,36-,38-,40+,41+,42+,45+,46-/m1/s1 checkY
    Key: QBAMBSAJEFIQBK-GJHUHQBXSA-N checkY
  • InChI=1S/C46H76O11/c1-13-34-18-16-14-15-17-28(4)42(51)45(12,54)43(52)32(8)40(50)31(7)39(49)30(6)38(48)27(3)19-22-37(47)55-41-29(5)35(21-20-34)56-46(33(41)9)24-23-26(2)36(57-46)25-44(10,11)53/h14-16,18-19,22,26-36,38,40-42,48,50-51,53-54H,13,17,20-21,23-25H2,1-12H3/b15-14+,18-16-,22-19+/t26-,27-,28+,29+,30+,31-,32-,33-,34+,35?,36-,38-,40+,41+,42+,45+,46-/m1/s1
    Key: QBAMBSAJEFIQBK-GJHUHQBXBC
  • Key: QBAMBSAJEFIQBK-GJHUHQBXSA-N
  • C[C@](C)(O)C[C@H]1O[C@@]2(CC[C@H]1C)O[C@H]3CC[C@@H](CC)/C=C\C=C\C[C@H](C)[C@H](O)[C@](C)(O)C(=O)[C@H](C)[C@@H](O)[C@H](C)C(=O)[C@@H](C)[C@H](O)[C@H](C)/C=C/C(=O)O[C@H]([C@H]2C)[C@H]3C
Properties
C45H74O11
Molar mass 791.062 g/mol
Hazards
Safety data sheet (SDS) MSDS at Fermentek
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
checkY verify (what is checkY☒N ?)

Oligomycins are macrolides created by Streptomyces that are strong antibacterial agents but are often poisonous to other organisms, including humans.

Function

[edit]

Oligomycins have use as antibiotics. However, in humans, they have limited or no clinical use due to their toxic effects on mitochondria and ATP synthase.[1]

Oligomycin A is an inhibitor of ATP synthase.[1] In oxidative phosphorylation research, it is used to prevent stage 3 (phosphorylating) respiration. Oligomycin A inhibits ATP synthase by blocking its proton channel (FO subunit), which is necessary for oxidative phosphorylation of ADP to ATP (energy production). The inhibition of ATP synthesis by oligomycin A will significantly reduce electron flow through the electron transport chain; however, electron flow is not stopped completely due to a process known as proton leak or mitochondrial uncoupling.[2] This process is due to facilitated diffusion of protons into the mitochondrial matrix through an uncoupling protein such as thermogenin, or UCP1.

Administering oligomycin to rats can result in very high levels of lactate accumulating in the blood and urine.[3]

Oligomycins[4]
  R1 R2 R3 R4 R5
Oligomycin A CH3 H OH H,H CH3
Oligomycin B CH3 H OH O CH3
Oligomycin C CH3 H H H,H CH3
Oligomycin D
(Rutamycin A) 		H H OH H,H CH3
Oligomycin E CH3 OH OH O CH3
Oligomycin F CH3 H OH H,H CH2CH3
Rutamycin B H H H H,H CH3
44-Homooligomycin A CH2CH3 H OH H,H CH3
44-Homooligomycin B CH2CH3 H OH O CH3

References

[edit]
Revisions and contributorsEdit on WikipediaRead on Wikipedia

Oligomycin

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from Grokipedia
Oligomycin is a family of closely related antibiotics, primarily consisting of oligomycins A, B, and C, isolated from the bacterium Streptomyces diastatochromogenes and first reported in 1954 as potent agents. These compounds feature a complex 26-membered macrolactone ring with spiroketal and enol ether functionalities, contributing to their . Oligomycin specifically targets the mitochondrial F1FO-, binding to the c-subunit ring in the membrane-embedded FO sector to block proton translocation through the enzyme's rotor, thereby inhibiting both ATP synthesis and during . This mechanism disrupts cellular energy production in eukaryotes, rendering oligomycin highly toxic to mammalian cells while conferring selective properties against certain fungi and yeasts. Discovered through screening of soil actinomycetes for compounds, oligomycin was initially characterized for its broad-spectrum inhibition of fungal growth, with the primary component, oligomycin A (molecular formula C45H74O11), comprising the majority of commercial preparations. In , biochemist Henry Lardy and colleagues identified its specific inhibitory effect on mitochondrial phosphoryl transfer, establishing oligomycin as a key tool for dissecting respiratory chain processes and function in isolated mitochondria and cell models. Subsequent structural elucidations in the 1960s and high-resolution crystallographic studies in the 2010s have refined understanding of its , revealing interactions with conserved residues in the c-ring that prevent rotational . Although not clinically used due to its eukaryotic , oligomycin remains indispensable in biomedical for assays measuring mitochondrial respiration, oxygen consumption rates, and extracellular acidification in contexts such as cancer metabolism, neurodegenerative diseases, and mitochondrial disorders like . Its application in has facilitated discoveries in , including the role of in and ischemia-reperfusion injury. Recent efforts have explored oligomycin analogs for targeted therapies, such as modulating mitochondrial permeability transition pores, highlighting its ongoing relevance in pharmacological innovation.

Discovery and Production

Discovery

Oligomycin was initially isolated in 1954 from a strain of the soil bacterium Streptomyces diastatochromogenes by Elizabeth McCoy, Robert M. Smith, and W.H. Peterson at the University of Wisconsin, who identified it as a active against a range of pathogenic fungi, including and . The compound was obtained through of the bacterial culture and subsequent purification, revealing its broad-spectrum inhibitory effects on fungal growth at low concentrations, with minimal impact on higher plants or animals at those levels. Early assays demonstrated that oligomycin also exhibited antibacterial activity specifically against , such as and , while showing little to no effect on Gram-negative species. In 1958, biochemist Henry Lardy and his colleagues at the University of Wisconsin further characterized oligomycin's biochemical properties, discovering its potent inhibition of and in isolated rat liver mitochondria. This finding positioned oligomycin as a valuable tool for metabolic studies, as it specifically blocked phosphoryl transfer reactions without disrupting electron transport or substrate oxidation at equivalent concentrations. Their work highlighted oligomycin's selectivity for mitochondrial activity, distinguishing it from other antibiotics and paving the way for its use in elucidating energy transduction mechanisms. In the late and early , detailed chemical separation efforts resolved the oligomycin complex into its primary components—oligomycins A, B, and C—confirming its classification as a antibiotic family produced by species. These key publications from the established oligomycin's dual role as both an antimicrobial agent and a biochemical probe, influencing subsequent research on and .

Biosynthesis and Production

Oligomycin is primarily produced by actinomycete bacteria of the genus , with key species including Streptomyces diastatochromogenes and . These microorganisms synthesize oligomycin as a during submerged fermentation in nutrient-rich media, such as those containing glucose, , and , under controlled aerobic conditions. The of oligomycin relies on a type I modular (PKS) system, which assembles the macrocyclic core through iterative condensation of -derived units. This pathway incorporates (as ), butyrate, and propionate units as building blocks, with specific incorporation patterns confirmed through studies using [1-¹³C]-propionate and [1-¹³C]-butyrate, leading to the characteristic 26-membered ring structure. In S. avermitilis, the responsible genetic cluster spans approximately 100 kb and includes the olmA encoding the multidomain PKS modules (OlmA1–OlmA7) for chain elongation and cyclization, along with post-PKS modification genes for oxidation and steps that yield variants like oligomycin A. Regulatory elements such as the LuxR-type activators olmRI and olmRII control cluster expression, ensuring coordinated assembly and tailoring to produce the bioactive oligomycin complex. Similar clusters have been identified in other producers, such as sp. FXY-T5, where disruptions confirm the PKS dependency. Industrial-scale production has been enhanced through fermentation optimization in actinomycetes, including to adjust (typically 7.0–7.5), (28–30°C), and carbon-to-nitrogen ratios, achieving up to several-fold increases in oligomycin yields compared to wild-type conditions. approaches, such as overexpression of regulatory genes or deletion of competing pathways, further boost titers in strains like S. avermitilis.

Chemical Structure and Properties

Molecular Structure

Oligomycin A, the primary component of the oligomycin complex, features a structure consisting of a 26-membered ring integrated with a bicyclic spiroketal moiety at positions C17–C22. This architecture is elaborated with a branched attached at the spiroketal, incorporating additional oxygen functionalities and alkyl substituents that define its overall scaffold. The molecular of oligomycin A is C45H74O11C_{45}H_{74}O_{11}, corresponding to a of 791.06 g/mol. Key functional groups include multiple hydroxyl groups at positions such as , C12, C15, and C26; carbonyls comprising a at C6 and the ; and linkages within the spiroketal. The molecule contains over 20 stereocenters, primarily along the and , which enforce a rigid conformation critical for its specificity. Variants within the oligomycin family, including oligomycins B and C, as well as D and E (known as rutamycins) and F, share the 26-membered and spiroketal core but differ in the R₁–R₅ substituents on the and . For example, oligomycin A bears an at C33, while oligomycin B features a at this position, altering the length and . Oligomycin D (rutamycin A), with formula C44H72O11C_{44}H_{72}O_{11}, has a methyl substituent adjacent to the spirocyclic center replaced by hydrogen relative to oligomycin A, resulting in a contracted alkyl chain. These structural variations influence potency and selectivity against .

Physical and Chemical Properties

Oligomycin A is typically obtained as a white to off-white crystalline powder. This form facilitates its handling in settings, where it is often stored desiccated to prevent moisture absorption. The compound exhibits low in , with values as low as 2 μg per 100 mL at 25°C, rendering it sparingly soluble in aqueous environments. In contrast, it is readily soluble in various organic solvents, including (up to 250 mg/mL), DMSO (50 mg/mL), acetone (50 mg/mL), and , which are commonly used for dissolution in experimental protocols. Oligomycin A has a melting point of 150–151°C. It demonstrates sensitivity to , necessitating protection during storage to avoid degradation, and is best maintained at -20°C in a dry, sealed environment for long-term stability, where lyophilized forms remain viable for up to 24 months. The compound is chemically stable across a broad range from 3 to 10 at 37°C for extended periods, such as 54 hours, but undergoes degradation via retro-aldol reactions in strong alkaline conditions.

Mechanism of Action

Inhibition of

Oligomycin specifically inhibits the mitochondrial by binding to the F₀ subunit, targeting the membrane-embedded c-ring composed of multiple c-subunits. This binding occurs at the interface between two adjacent c-subunits, where oligomycin interacts primarily through hydrophobic contacts with residues such as Phe64, Ala56, and Ala60, while forming a with the essential Glu59 residue via a bridging molecule. By locking Glu59 in a semiclosed conformation, oligomycin shields the proton-binding site from the aqueous half-channel, thereby blocking proton translocation through the F₀ channel. This inhibition disrupts the rotary mechanism of , preventing the conformational changes necessary for ATP synthesis. In the rotor-stator model, proton flow through F₀ drives the rotation of the c-ring relative to the , inducing cyclic conformational changes in the F₁ domain that facilitate ADP to ATP. Oligomycin halts c-ring rotation in both directions by impeding proton movement, thus abolishing the torque generation required for these conformational shifts without directly affecting the catalytic sites in F₁. A key characteristic of oligomycin's action is its selectivity for the intact F₀F₁ complex; it exerts no inhibitory effect on by the isolated F₁ sector, which lacks the F₀ component. In contrast, within the fully assembled enzyme, oligomycin completely blocks both ATP synthesis and hydrolysis activities, underscoring the dependence on F₀ integrity for sensitivity. This distinction arises because oligomycin's is exclusively within the F₀ domain, confirming its role as a specific F₀-targeted inhibitor. Structural insights from have elucidated these interactions at near-atomic resolution. For instance, a 2012 crystal structure analysis of mitochondrial revealed oligomycin spanning the c-ring surface, contacting two c-subunits and explaining its potent blockade of proton flux. These findings have framed a conserved drug-binding pocket in the c-ring, informing the design of related inhibitors.

Effects on

Oligomycin inhibits by binding to the F₀ subunit of , preventing proton translocation and thereby halting ATP production coupled to the . This blockage creates a backlog in the proton gradient across the , reducing the flow of electrons through the chain and effectively stopping aerobic ATP synthesis. In response to this inhibition, mitochondria may exhibit compensatory proton leak mechanisms to mitigate the buildup of , particularly in tissues expressing uncoupling proteins such as in , where the leak allows continued electron transport despite the blockade. Overall, oligomycin treatment leads to a marked reduction in cellular oxygen consumption as respiration is curtailed, prompting a metabolic shift toward anaerobic glycolysis with increased lactate production to sustain ATP levels. The effects of oligomycin on isolated mitochondria are often reversible upon removal of the inhibitor or application of reversing agents like ionophores, restoring activity and respiratory function. However, in vivo administration results in cumulative mitochondrial damage, including inflammatory responses and sustained bioenergetic impairment, due to prolonged exposure and secondary cellular stresses.

Biological Effects and Toxicity

Antibacterial and Antifungal Activity

Oligomycin exhibits no significant antibacterial activity against Gram-positive or due to its specificity for mitochondrial , which is absent in prokaryotes, and differences in the bacterial enzyme structure that prevent effective inhibition. The compound demonstrates potent antifungal effects, particularly against phytopathogenic fungi such as Magnaporthe oryzae (causing rice blast) and , with minimum inhibitory concentrations (MICs) in the range of 1–4 μg/mL for various strains. In these sensitive fungal species, oligomycin suppresses mycelial growth and spore germination by interfering with mitochondrial ATP production, leading to energy depletion and halted cellular processes. Oligomycin's antimicrobial spectrum is limited to eukaryotes with mitochondria, showing little to no efficacy against bacteria. Originally identified in 1954 as an antifungal agent produced by Streptomyces, it has been explored historically for agricultural applications against plant pathogens and in early antibiotic screening programs.

Toxicity in Mammals

Oligomycin exhibits high toxicity in mammals primarily due to its inhibition of mitochondrial ATP synthase, which disrupts oxidative phosphorylation across all cell types, leading to energy failure in vital organs. In rats, the intraperitoneal LDLo (lowest lethal dose) is approximately 0.5 mg/kg, indicating acute lethality at low doses. This universal mitochondrial blockade results in a profound reduction in whole-body oxygen consumption by about 50% at sublethal doses, alongside rapid ATP depletion that compromises cellular homeostasis. Acute exposure manifests as metabolic disturbances, including from elevated blood and tissue lactate levels due to shunted and impaired aerobic respiration. Systemic symptoms in animal models include , reduced renal urea excretion, increased plasma , anorexia, , and central nervous system depression, reflecting multi-organ stress from energy deficits. These effects stem from oligomycin's blockade of respiratory chain function, exacerbating anaerobic metabolism and acid-base imbalance. Cardiotoxicity is a prominent concern, with oligomycin inducing dose-dependent hemodynamic , including severe (decreases in exceeding 40 mmHg at 1 mg/kg), ( reductions over 150 bpm), and diminished cardiac contractility. At higher doses, this progresses to potential irreversible myocardial damage through sustained mitochondrial dysfunction in cardiomyocytes, which rely heavily on ATP for contractility. There is no specific for oligomycin poisoning; management is limited to supportive care, such as fluid resuscitation and monitoring for cardiovascular collapse.

Applications

Research Uses

Oligomycin serves as a primary tool in biochemical research to investigate and mitochondrial function, particularly in isolated mitochondria and submitochondrial particles. By specifically inhibiting the F₀ subunit of , it allows researchers to dissect the contributions of ATP synthesis to overall respiratory activity, enabling precise measurements of proton motive force and energy coupling in organelles. This application has been instrumental in elucidating the mechanisms of mitochondrial since its adoption in early studies of respiratory control. In assays for ATP synthase activity, oligomycin is routinely employed to confirm enzyme specificity and quantify hydrolytic or synthetic functions. For instance, in spectrophotometric protocols, addition of oligomycin inhibits ATP-driven proton translocation, providing a baseline for coupled respiration and validating the assay's sensitivity to F₁F₀ interactions. It is also used in high-throughput screens to evaluate respiratory chain deficiencies by blocking ATP-linked oxygen consumption, thus isolating electron transport system capacity independent of . Furthermore, oligomycin facilitates studies of production in mitochondria, where its inhibition of induces generation at complex I or III sites, aiding in the mapping of ROS sources during metabolic stress. As a tool in , oligomycin induces metabolic stress by halting ATP production via inhibition, which is leveraged to explore cellular responses such as activation or pathways. It is particularly valuable for analyzing uncoupling proteins (UCPs), where oligomycin-insensitive proton leak is measured to assess UCP-mediated dissipation of the proton gradient, distinguishing it from ATP synthase-driven respiration. In these contexts, oligomycin helps quantify uncoupling efficiency in models of or . Typical protocols for mitochondrial preparations involve oligomycin concentrations of 1-10 μM, which effectively block without broadly disrupting other respiratory components, though lower doses (0.5-1 μM) are used for subtle modulation in intact cells. These ranges ensure reversible inhibition in short-term experiments, allowing for titratable effects on .

Potential Therapeutic Uses

Oligomycin has been investigated for its potential in cancer therapy due to its ability to selectively target rapidly dividing cancer cells that depend heavily on for energy production. By inhibiting , oligomycin disrupts mitochondrial ATP synthesis, leading to reduced cell viability and proliferation in various cancer models. For instance, in (), oligomycin demonstrates dose-dependent inhibition of in MDA-MB-231 and BT-549 cell lines, as shown by CCK-8 assays and colony formation experiments, while also impairing mitochondrial and ATP levels. , oligomycin administration significantly reduced xenograft tumor volumes in nude mice compared to controls, highlighting its antitumor efficacy when targeting metabolic proteins like ATP5MF. Additionally, oligomycin shows promise against cancer stem cells (CSCs) in and models by blocking Complex V of the , thereby limiting CSC survival and stemness, particularly in combination with inhibitors like . In the context of antifungal treatments, oligomycin's historical identification as an agent stems from its inhibition of in fungal pathogens such as , , and . Its potential as an for resistant fungal strains arises from observations that ATP synthase inhibitors can enhance the efficacy of existing antifungals by disrupting energy-dependent resistance mechanisms, though this application remains exploratory and constrained by oligomycin's broad eukaryotic targeting. Studies on mitochondrial diseases, particularly ATP synthase-related disorders like neuropathy, ataxia, and retinitis pigmentosa (NARP) syndrome caused by MT-ATP6 mutations, have utilized oligomycin to model OXPHOS deficiencies and evaluate corrective strategies. In transmitochondrial cybrids harboring the 8993T→G NARP mutation, oligomycin exposure (0.6 nM) reduces cell viability to 15% at 72 hours, but supplementation with α-ketoglutarate/aspartate restores survival to 75% by maintaining ATP levels, suggesting oligomycin's utility in identifying metabolic therapies for such conditions. This approach underscores investigational potential for oligomycin derivatives in modulating ATP synthase defects in mitochondrial encephalomyopathies. Despite these prospects, oligomycin lacks approved human clinical uses as of 2025, primarily due to its systemic toxicity, including induction of cardiac , , and renal damage in animal models. Ongoing research focuses on developing analogs to mitigate these side effects while preserving therapeutic activity; for example, new oligomycin derivatives have been synthesized to inhibit anchorage-independent growth in cells, and spiropiperidine-based structures target mitochondrial permeability transition pores with reduced off-target effects. Recent reviews emphasize chemical diversification of oligomycin A to enhance its bioactivity and for anticancer and applications.

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