56 research outputs found

    Tribological behaviour of a356/sic nanocomposite

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    The paper presents tribological behaviour of aluminium nanocomposite A356/SiC produced by the compocasting process with mechanical alloying preprocessing (ball milling). Tribological tests were performed on tribometer with block-on-disc contact geometry under lubricated sliding conditions. Influence of amount of silicon carbide reinforcement (0, 0.2, 0.3 and 0.5 wt.%) on wear rate was investigated in the following testing conditions: sliding speed of 0.25 and 1.0 m/s, normal load of 40 N and 100 N and at sliding distance of 1000 m. Analysis of worn surface of nanocomposites was performed by using SEM equipped with EDS

    Tribological behaviour of a356/sic nanocomposite

    Get PDF
    The paper presents tribological behaviour of aluminium nanocomposite A356/SiC produced by the compocasting process with mechanical alloying preprocessing (ball milling). Tribological tests were performed on tribometer with block-on-disc contact geometry under lubricated sliding conditions. Influence of amount of silicon carbide reinforcement (0, 0.2, 0.3 and 0.5 wt.%) on wear rate was investigated in the following testing conditions: sliding speed of 0.25 and 1.0 m/s, normal load of 40 N and 100 N and at sliding distance of 1000 m. Analysis of worn surface of nanocomposites was performed by using SEM equipped with EDS

    Ultrafast 2D-IR spectroscopy of [NiFe] hydrogenase from E. coli reveals the role of the protein scaffold in controlling the active site environment

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    Ultrafast two-dimensional infrared (2D-IR) spectroscopy of Escherichia coli Hyd-1 (EcHyd-1) reveals the structural and dynamic influence of the protein scaffold on the Fe(CO)(CN)2 unit of the active site. Measurements on as-isolated EcHyd-1 probed a mixture of active site states including two, which we assign to Nir-SI/II, that have not been previously observed in the E. coli enzyme. Explicit assignment of carbonyl (CO) and cyanide (CN) stretching bands to each state is enabled by 2D-IR. Energies of vibrational levels up to and including two-quantum vibrationally excited states of the CO and CN modes have been determined along with the associated vibrational relaxation dynamics. The carbonyl stretching mode potential is well described by a Morse function and couples weakly to the cyanide stretching vibrations. In contrast, the two CN stretching modes exhibit extremely strong coupling, leading to the observation of formally forbidden vibrational transitions in the 2D-IR spectra. We show that the vibrational relaxation times and structural dynamics of the CO and CN ligand stretching modes of the enzyme active site differ markedly from those of a model compound K[CpFe(CO)(CN)2] in aqueous solution and conclude that the protein scaffold creates a unique biomolecular environment for the NiFe site that cannot be represented by analogy to simple models of solvation

    The mechanism of catalysis by type-II NADH : quinone oxidoreductases

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    Type II NADH:quinone oxidoreductase (NDH-2) is central to the respiratory chains of many organisms. It is not present in mammals so may be exploited as an antimicrobial drug target or used as a substitute for dysfunctional respiratory complex I in neuromuscular disorders. NDH-2 is a single-subunit monotopic membrane protein with just a flavin cofactor, yet no consensus exists on its mechanism. Here, we use steady-state and pre-steady-state kinetics combined with mutagenesis and structural studies to determine the mechanism of NDH-2 from Caldalkalibacillus thermarum. We show that the two substrate reactions occur independently, at different sites, and regardless of the occupancy of the partner site. We conclude that the reaction pathway is determined stochastically, by the substrate/product concentrations and dissociation constants, and can follow either a ping-pong or ternary mechanism. This mechanistic versatility provides a unified explanation for all extant data and a new foundation for the development of therapeutic strategies

    A Reference High-Pressure CO2 Adsorption Isotherm for Ammonium ZSM-5 Zeolite: Results of an Interlaboratory Study

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    © 2018, The Author(s). This paper reports the results of an international interlaboratory study led by the National Institute of Standards and Technology (NIST) on the measurement of high-pressure surface excess carbon dioxide adsorption isotherms on NIST Reference Material RM 8852 (ammonium ZSM-5 zeolite), at 293.15 K (20 °C) from 1 kPa up to 4.5 MPa. Eleven laboratories participated in this exercise and, for the first time, high-pressure adsorption reference data are reported using a reference material. An empirical reference equation nex=d(1+exp[(-ln(P)+a)/b])c, [nex-surface excess uptake (mmol/g), P-equilibrium pressure (MPa), a = −6.22, b = 1.97, c = 4.73, and d = 3.87] along with the 95% uncertainty interval (Uk = 2 = 0.075 mmol/g) were determined for the reference isotherm using a Bayesian, Markov Chain Monte Carlo method. Together, this zeolitic reference material and the associated adsorption data provide a means for laboratories to test and validate high-pressure adsorption equipment and measurements. Recommendations are provided for measuring reliable high-pressure adsorption isotherms using this material, including activation procedures, data processing methods to determine surface excess uptake, and the appropriate equation of state to be used

    Cryo-EM structures of complex I from mouse heart mitochondria in two biochemically defined states.

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    Complex I (NADH:ubiquinone oxidoreductase) uses the reducing potential of NADH to drive protons across the energy-transducing inner membrane and power oxidative phosphorylation in mammalian mitochondria. Recent cryo-EM analyses have produced near-complete models of all 45 subunits in the bovine, ovine and porcine complexes and have identified two states relevant to complex I in ischemia-reperfusion injury. Here, we describe the 3.3-Å structure of complex I from mouse heart mitochondria, a biomedically relevant model system, in the 'active' state. We reveal a nucleotide bound in subunit NDUFA10, a nucleoside kinase homolog, and define mechanistically critical elements in the mammalian enzyme. By comparisons with a 3.9-Å structure of the 'deactive' state and with known bacterial structures, we identify differences in helical geometry in the membrane domain that occur upon activation or that alter the positions of catalytically important charged residues. Our results demonstrate the capability of cryo-EM analyses to challenge and develop mechanistic models for mammalian complex I

    Structure of inhibitor-bound mammalian complex I

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    Funder: The Swedish National Infrastructure for Computing (SNIC, 2019/2-3) UK National Electron Bio-Imaging Centre (eBIC) at the Diamond Light Source, proposal EM16309, funded by the Wellcome Trust, MRC and BBSRCAbstract: 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

    Fault analysis of gearboxes in open pit mine

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    © 2019 Published by the Serbian Academic Center. The paper presents the results of testing gearboxes in coal open pit mine which have been damaged by various mechanisms. Gearboxes, as constituents of belt conveyors, bucket-wheel excavators and bucket chain excavators and spreaders, are the most loaded segments of drive units the functionality of which affects the operation of complete coal and overburden systems. Therefore, special attention has to be paid to their condition so that the analysis of relevant condition indicators could lead to correct conclusions as to their functionality, as well as point to the factors causing their fault. Tests were carried out on 95 gearboxes throughout 2017, during general repairs at Drmno mine workshop. After examination, all identified failures were illustrated with an appropriate photo, classified according to the appropriate standard, and described in the form of manifestation and cause. The research has shown that the most dominant were faults of bearings and lubrication, whether seals and cuffs or a thin hermetic layer between the housing and covers. In addition, some of the faults happened on gears and toothed and stepped shafts. Major irregularities in operation, resulting from damage to gearbox elements, are show by fault tree analysis (FTA)
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