Bacterial FOF1 ATP: Nanomotor for ATP Synthesis and Hydrolysis and Mechanism of Interaction with the Macrolide Antibiotic Oligomycin A

2020 ◽  
Vol 10 (6) ◽  
pp. 483-494
Author(s):  
A. A. Vatlin ◽  
V. N. Danilenko
Keyword(s):  
Macrolide Antibiotic ◽  
Atp Synthesis ◽  
Oligomycin A ◽  
Mechanism Of Interaction

scholarly journals A comparison of the effects of NN′-dicyclohexylcarbodi-imide, oligomycin A and aurovertin on energy-linked reactions in mitochondria and submitochondrial particles

1968 ◽  
Vol 108 (3) ◽  
pp. 445-456 ◽  
Author(s):  
A. M. Roberton ◽  
Caroline T. Holloway ◽  
I G Knight ◽  
R B Beechey
Keyword(s):  
Potent Inhibitor ◽  
Atp Synthesis ◽  
Mitochondrial Fraction ◽  
Optimum Concentration ◽  
Submitochondrial Particles ◽  
Nicotinamide Nucleotide Transhydrogenase ◽  
Oligomycin A ◽  
Submitochondrial Particle ◽  
Site Of Action ◽  
Stimulation Of

1. The effects of dicyclohexylcarbodi-imide, oligomycin A and aurovertin on enzyme systems related to respiratory-chain phosphorylation were compared. Dicyclohexylcarbodi-imide and oligomycin A have very similar functional effects, giving 50% inhibition of ATP-utilizing and ATP-generating systems at concentrations below 0·8nmole/mg. of submitochondrial-particle protein. Aurovertin is a more potent inhibitor of ATP synthesis, giving 50% inhibition at 0·2nmole/mg. of protein. However, aurovertin is a less potent inhibitor of ATP-utilizing systems: the ATP-driven energy-linked nicotinamide nucleotide transhydrogenase is 50% inhibited at 3·0nmoles/mg. of protein and the ATP-driven reduction of NAD+ by succinate is 50% inhibited at 0·95nmole/mg. of protein. 2. With EDTA-particles (prepared by subjecting mitochondria to ultrasonic radiation at pH9 in the presence of 2mm-EDTA) the maximum stimulation of the ATP-driven partial reactions is effected by similar concentrations of oligomycin A and dicylcohexylcarbodi-imide, but the latter is less effective. The stimulatory effects of suboptimum concentrations of dicyclohexylcarbodi-imide and oligomycin A are additive. Aurovertin does not stimulate these reactions or interfere with the stimulation by the other inhibitors. 3. Dicyclohexylcarbodi-imide and oligomycin A stimulate the aerobic energy-linked nicotinamide nucleotide transhydrogenase of EDTA-particles, but the optimum concentration is higher than that required for the ATP-driven partial reactions. Aurovertin has no effect on this reaction. 4. The site of action of dicyclohexylcarbodi-imide is in CF0, the mitochondrial fraction that confers oligomycin sensitivity on F1 mitochondrial adenosine triphosphatase.

Isolation, identification, and antifungal activity of a macrolide antibiotic, oligomycin A, produced by Streptomyces libani

1999 ◽  
Vol 77 (6) ◽  
pp. 850-858 ◽  
Author(s):  
Beom Seok Kim ◽  
Surk Sik Moon ◽  
Byung Kook Hwang
Keyword(s):  
Antifungal Activity ◽  
Magnaporthe Grisea ◽  
Macrolide Antibiotic ◽  
Oryza Sativa L ◽  
Plant Diseases ◽  
Broth Culture ◽  
Molecular Formula ◽  
Leaf Blast ◽  
Cucumis Sativus L ◽  
Oligomycin A

The antibiotic As1A, strongly inhibitory to Phytophthora capsici Leonian in vitro and in vivo, was isolated from the broth culture of Streptomyces libani Baldacci & Grein using various chromatographic procedures. The molecular formula of the antibiotic As1A was deduced to be C45H74O11 (M+H, m/z 791.5307) by high resolution fast atom bombardment - mass spectroscopy. The analysis of 1H-NMR (nuclear magnetic resonance) and 13C-NMR spectroscopy, DEPT experiment, and two-dimensional NMR spectral data revealed that the antibiotic is a macrolide antibiotic having a 26-membered alpha, beta-unsaturated macrolactone ring with a conjugated diene fused to a bicyclic spiroketal. Based on the comparison of NMR data and other chemical properties, the antibiotic As1A turned out to have the same structure as oligomycin A. The antibiotic As1A showed a high level of inhibitory activity against Botrytis cinerea Pers.: Pers., Cladosporium cucumerinum Ellis & Arthur, Colletotrichum lagenarium (C.P. Robin) Berkhout, Magnaporthe grisea (Herb.) Barr, and P. capsici, ranging from 3 to 5 µg·mL-1 of MICs. However, no antimicrobial activity was found against yeasts and bacteria. In further evaluation under greenhouse conditions, developments of the Phytophthora disease, anthracnose, and leaf blast were markedly inhibited on pepper (Capsicum annuum L. cv. Hanbyul), cucumber (Cucumis sativus L. cv. Baekrokdadaki), and rice (Oryza sativa L. cv. Nakdong) plants by treatments with the antibiotic As1A, respectively. Control efficacies of the antibiotic As1A against these plant diseases were in general similar to those of metalaxyl, chlorothalonil, and tricyclazole. The antibiotic As1A did not show any phytotoxicity on pepper, cucumber, and rice plants even at 500 µg·mL-1.Key words: Streptomyces libani, oligomycin A, antifungal activity, plant disease control.

Ultrastructural autoradiography of L6 skeletal-muscle cells exposed to a tritiated macrolide antibiotic (LY237216) in vitro

1992 ◽  
Vol 50 (1) ◽  
pp. 612-613
Author(s):  
S.L. White ◽  
C.B. Jensen ◽  
D.D. Giera ◽  
D.A. Laska ◽  
M.N. Novilla ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Quantitative Analysis ◽  
Macrolide Antibiotic ◽  
Circle Method ◽  
Apical Surface ◽  
Polycarbonate Membrane ◽  
L6 Cells ◽  
Low Viscosity ◽  
Erythromycin A

In vitro exposure to LY237216 (9-Deoxo-11-deoxy-9,11-{imino[2-(2-methoxyethoxy)ethylidene]-oxy}-(9S)-erythromycin), a macrolide antibiotic, was found to induce cytoplasmic vacuolation in L6 skeletal muscle myoblast cultures (White, S.L., unpubl). The present study was done to determine, by autoradiographic quantitative analysis, the subcellular distribution of 3H-LY237216 in L6 cells.L6 cells (ATCC, CRL 1458) were cultured to confluency on polycarbonate membrane filters (Millipore Corp., Bedford, MA) in M-199 medium (GIBCO® Labs) with 10% fetal bovine serum. The cells were exposed from the apical surface for 1-hour to unlabelled-compound (0 μCi/ml) or 50 (μCi/ml of 3H-LY237216 at a compound concentration of 0.25 mg/ml. Following a rapid rinse in compound-free growth medium, the cells were slam-frozen against a liquid nitrogen cooled, polished copper block in a CF-100 cryofixation unit (LifeCell Corp., The Woodlands, TX). Specimens were dried in the MDD-C Molecular Distillation Drier (LifeCell Corp.), vapor osmicated and embedded in Spurrs low viscosity resin. Ultrathin sections collected on formvar coated stainless steel grids were counter-stained, then individually mounted on corks. A monolayer of Ilford L4 nuclear emulsion (Polysciences, Inc., Warrington, PA) was placed on the sections, utilizing a modified “loop method”. The emulsions were exposed for 7-weeks in a light-tight box at 4°C. Autoradiographs were developed in Microdol-X developer and examined on a Philips EM410LS transmission electron microscope. Quantitative analysis of compound localization employed the point and circle approach of Williams; incorporating the probability circle method of Salpeter and McHenry.

Effects of Neuroactive Amino Acids Derivatives on Cardiac and Cerebral Mitochondria and Endothelial functions in Animals Exposed to Stress

2017 ◽  
Vol 2 (2) ◽  
pp. 34
Author(s):  
TA Popova ◽  
II Prokofiev ◽  
IS Mokrousov ◽  
Valentina Perfilova ◽  
AV Borisov ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Blood Pressure ◽  
Platelet Aggregation ◽  
Atp Synthesis ◽  
Elevated Concentration ◽  
Blood Pressure Monitor ◽  
Pressure Monitor ◽  
Griess Reagent ◽  
Arterial Blood ◽  
Endothelial Functions

Introduction: To study the effects of glufimet, a new derivative of glutamic acid, and phenibut, a derivative of γ-aminobutyric acid (GABA), on cardiac and cerebral mitochondria and endothelial functions in animals following exposure to stress and inducible nitric oxide synthase (iNOS) inhibition. Methods: Rats suspended by their dorsal cervical skin fold for 24 hours served as the immobilization and pain stress model. Arterial blood pressure was determined using a non-invasive blood pressure monitor. Mitochondrial fraction of heart and brain homogenates were isolated by differential centrifugation and analysed for mitochondrial respiration intensity, lipid peroxidation (LPO) and antioxidant enzyme activity using polarographic method. The concentrations of nitric oxide (NO) terminal metabolites were measured using Griess reagent. Hemostasis indices were evaluated. Platelet aggregation was estimated using modified version of the Born method described by Gabbasov et al., 1989. Results: The present study demonstrated that stress leads to an elevated concentration of NO terminal metabolites and LPO products, decreased activity of antioxidant enzymes, reduced mitochondrial respiratory function, and endothelial dysfunction. Inhibition of iNOS by aminoguanidine had a protective effect. Phenibut and glufimet inhibited a rise in stress-induced nitric oxide production. This resulted in enhanced coupling of substrate peroxidation and ATP synthesis. The reduced LPO processes caused by glufimet and phenibut normalized the endothelial function which was proved by the absence of average daily blood pressure (BP) elevation episodes and a significant increase in platelet aggregation level. Conclusion: Glufimet and phenibut restrict the harmful effects of stress on the heart and brain possibly by modulating iNOS activity.

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