Electromagnetic Energy Coupling Mechanism on Cables and Systems - A Comparison Composite Aircraft Versus Metal Aircraft and Impact on Testing Procedure

2011 ◽  
Vol 4 (2) ◽  
pp. 672-680 ◽  
Author(s):  
Fidele Moupfouma
Keyword(s):  
Energy Coupling ◽  
Testing Procedure ◽  
Electromagnetic Energy ◽  
Coupling Mechanism

scholarly journals ELECTRON MICROSCOPE HISTOCHEMICAL EVIDENCE FOR A PARTIAL OR TOTAL BLOCK OF THE TRICARBOXYLIC ACID CYCLE IN THE MITOCHONDRIA OF PRESYNAPTIC AXON TERMINALS

1971 ◽  
Vol 51 (1) ◽  
pp. 216-222 ◽  
Author(s):  
Ferenc Hajós ◽  
Sándor Kerpel-Fronius
Keyword(s):  
Tricarboxylic Acid Cycle ◽  
Energy Coupling ◽  
Tricarboxylic Acid ◽  
Synaptic Function ◽  
Coupling Mechanism ◽  
Succinate Oxidation ◽  
Acid Cycle ◽  
Axon Terminals ◽  
Massive Accumulation

Respiration-linked, massive accumulation of Sr2+ is used to reveal the coupled oxidation of pyruvate, α-oxoglutarate, succinate, and malate by in situ mitochondria. All of these substrates were actively oxidized in the dendritic and perikaryal mitochondria, but no α-oxoglutarate or succinate utilization could be demonstrated in the mitochondria of the presynaptic axon terminals. A block at an early step of α-oxoglutarate and succinate oxidation is proposed to account for the negative histochemical results, since the positive reaction with pyruvate and malate proves that these mitochondria possess an intact respiratory chain and energy-coupling mechanism essential for Sr2+ accumulation. This indicates that the mitochondria in the axon terminals would be able to generate energy for synaptic function with at least some of the respiratory substrates. With regard to the block in the tricarboxylic acid cycle, the oxaloacetate necessary for citrate formation is suggested to be provided by fixation of CO2 into some of the pyruvate.

scholarly journals No Single Irreplaceable Acidic Residues in the Escherichia coli Secondary Multidrug Transporter MdfA

2006 ◽  
Vol 188 (15) ◽  
pp. 5635-5639 ◽  
Author(s):  
Nadejda Sigal ◽  
Shahar Molshanski-Mor ◽  
Eitan Bibi
Keyword(s):  
Escherichia Coli ◽  
Critical Role ◽  
Energy Coupling ◽  
Major Facilitator Superfamily ◽  
Multidrug Transporter ◽  
Coupling Mechanism ◽  
Acidic Residues ◽  
Major Facilitator ◽  
Mfs Transporters ◽  
Solute Transporters

ABSTRACT The largest family of solute transporters (major facilitator superfamily [MFS]) includes proton-motive-force-driven secondary transporters. Several characterized MFS transporters utilize essential acidic residues that play a critical role in the energy-coupling mechanism during transport. Surprisingly, we show here that no single acidic residue plays an irreplaceable role in the Escherichia coli secondary multidrug transporter MdfA.

High Performance Actuation System Enabled by Energy Coupling Mechanism

2013 ◽  
Author(s):  
Daniel Skelton ◽  
Shaoping Xiong ◽  
John Lumkes ◽  
Farid Breidi
Keyword(s):  
High Performance ◽  
Energy Coupling ◽  
Coupling Mechanism ◽  
Actuation System

scholarly journals Coupling mechanism of materials and screen surface motion in multi-stage variable inclination equal thickness screening process

2021 ◽  
Vol 2076 (1) ◽  
pp. 012087
Author(s):  
Long Huang ◽  
Yuemin Zhao ◽  
Yadong Zhang ◽  
Miao Pan ◽  
Haishen Jiang ◽  
...  
Keyword(s):  
High Speed ◽  
Production Capacity ◽  
Energy Coupling ◽  
Coupling Mechanism ◽  
Screening Process ◽  
Multi Stage ◽  
Motion Speed ◽  
Equal Thickness ◽  
Load Conditions ◽  
Screen Surface

Abstract Multi-stage variable inclination equal-thickness screen (MSVIETS) is widely used in separating coal and mineral particles because of its large production capacity and good screening performance. In this study, the kinematic characteristics of infeed and outfeed ends surface under the conditions of load and no load was investigated by using a high-speed camera analysis system. The motion speed of the screen surface at the infeed end was approximately 5 times higher under load than under no-load conditions, and motion speed of the screen surface at the outfeed end was approximately 4 times higher than under no-load conditions. The mechanism of coupled motion of material and screen surface in the process of multi-stage variable inclination equal thickness screening was elucidated, and the energy coupling transfer law was “strong in and weak out”.

scholarly journals Structure of inhibitor-bound mammalian complex I

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Hannah R. Bridges ◽  
Justin G. Fedor ◽  
James N. Blaza ◽  
Andrea Di Luca ◽  
Alexander Jussupow ◽  
...  
Keyword(s):  
Complex I ◽  
Energy Coupling ◽  
Competitive Inhibitor ◽  
Nadh:Ubiquinone Oxidoreductase ◽  
Mouse Heart ◽  
Coupling Mechanism ◽  
Substrate Reduction ◽  
Mitochondrial Inner Membrane ◽  
Respiratory Complex I ◽  
Ubiquinone Binding

Abstract Respiratory complex I (NADH:ubiquinone oxidoreductase) captures the free energy from oxidising NADH and reducing ubiquinone to drive protons across the mitochondrial inner membrane and power oxidative phosphorylation. Recent cryo-EM analyses have produced near-complete models of the mammalian complex, but leave the molecular principles of its long-range energy coupling mechanism open to debate. Here, we describe the 3.0-Å resolution cryo-EM structure of complex I from mouse heart mitochondria with a substrate-like inhibitor, piericidin A, bound in the ubiquinone-binding active site. We combine our structural analyses with both functional and computational studies to demonstrate competitive inhibitor binding poses and provide evidence that two inhibitor molecules bind end-to-end in the long substrate binding channel. Our findings reveal information about the mechanisms of inhibition and substrate reduction that are central for understanding the principles of energy transduction in mammalian complex I.

scholarly journals Semiquinone intermediates are involved in the energy coupling mechanism of E. coli complex I

2015 ◽  
Vol 1847 (8) ◽  
pp. 681-689 ◽  
Author(s):  
Madhavan Narayanan ◽  
Steven A. Leung ◽  
Yuta Inaba ◽  
Mahmoud M. Elguindy ◽  
Eiko Nakamaru-Ogiso
Keyword(s):  
Complex I ◽  
Energy Coupling ◽  
Coupling Mechanism ◽  
E Coli
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