53 research outputs found

    Fire performance of phase change material enhanced plasterboard

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    Sustainable construction materials are increasingly being used to reduce the carbon footprint of modern buildings. These materials have the potential to change the fire dynamics of compartments by altering the compartment energy balance however there is little quantitative understanding of how these materials behave in the event of a real fire. The changes in fire dynamics may be due to increased fuel load in a compartment, reduced time to failure or promotion of flame spread. The objective of this research is to quantify how Phase Change Materials (PCMs) perform in realistic fire scenarios. It was found that a plasterboard product containing microencapsulated PCMs will behave similarly to a charring solid and have the potential to contribute significant fuel to a compartment fire but that they maintain integrity for the duration of flaming period. The critical heat flux for this product was determined in the cone calorimeter to be 17.5 ± 2.5 kW m−2, the peak heat release rate and mass loss rate ranged from 60.2 kW m−2 to 107 kW m−2 and 1.88 g s−1 m−2 to 8.47 g s−1 m−2 respectively for exposures between 20 kW m−2 and 70 kW m−2. Sample orientation was found to increase the peak heat release rate by up to 25%, whilst having little to no effect on the mass loss rate. These parameters, in addition to the in-depth temperature evolution and ignition properties, can be used as design criteria for balancing energy savings with quantified fire performance

    Catalysis in fumarate reductase

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    AbstractIn the absence of oxygen many bacteria are able to utilise fumarate as a terminal oxidant for respiration. In most known organisms the fumarate reductases are membrane-bound iron-sulfur flavoproteins but Shewanella species produce a soluble, periplasmic flavocytochrome c3 that catalyses this reaction. The active sites of all fumarate reductases are clearly conserved at the structural level, indicating a common mechanism. The structures of fumarate reductases from two Shewanella species have been determined. Fumarate, succinate and a partially hydrated fumarate ligand are found in equivalent locations in different crystals, tightly bound in the active site and close to N5 of the FAD cofactor, allowing identification of amino acid residues that are involved in substrate binding and catalysis. Conversion of fumarate to succinate requires hydride transfer from FAD and protonation by an active site acid. The identity of the proton donor has been open to question but we have used structural considerations to suggest that this function is provided by an arginine side chain. We have confirmed this experimentally by analysing the effects of site-directed mutations on enzyme activity. Substitutions of Arg402 lead to a dramatic loss of activity whereas neither of the two active site histidine residues is required for catalysis
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