Ricerc@Sapienza

Interaction of two redox enzymes of Escherichia coli, cytochrome bo3 and cytochrome bd-I, with ammonium sulfate/ammonia at pH 7.0 and 8.3 was studied using high-resolution respirometry and absorption spectroscopy. At pH 7.0, the oxygen reductase activity of none of the enzymes is affected by the ligand. At pH 8.3, cytochrome bo3 is inhibited by the ligand, with 40% maximum inhibition at 100 mM (NH4 )2SO4 . In contrast, the activity of cytochrome bd-I at pH 8.3 increases with increasing the ligand concentration, the largest increase (140%) is observed at 100 mM (NH4 )2SO4 .

When water-ammonia absorption machines are used as heat pumps, the main problems can be found in the components operating at a high pressure (generator-condenser); the increase in temperature with respect to the exertion as refrigerator generates particular conditions that might unbalance the decomposition of ammonia into nitrogen. A decrease in the rate of the refrigerating fluid NH3 in the condenser and evaporator occurs, hence of the performance coefficient of the heat pump with an increased risk of the potential generation of explosive mixtures due to the presence of the hydrogen.