The first activation study of a bacterial carbonic anhydrase (CA). The thermostable ?±-CA from Sulfurihydrogenibium yellowstonense YO3AOP1 is highly activated by amino acids and amines

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Anion inhibition studies of the fastest carbonic anhydrase (CA) known the extremo-CA from the bacterium Sulfurihydrogenibium azorense

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The extremo-?±-carbonic anhydrase from the thermophilic bacterium Sulfurihydrogenibium azorense is highly inhibited by sulfonamides

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The alpha-carbonic anhydrase from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1 is highly susceptible to inhibition by sulfonamides

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Anion inhibition studies of an α-carbonic anhydrase from the thermophilic bacterium Sulfurihydrogenibium yellowstonense YO3AOP1

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Physiological and ultrastructural effects of acute ozone fumigation in the lichen Xanthoria parietina: the role of parietin and hydration state

The physiological and ultrastructural effects induced by acute exposure to ozone (O3) were investigated in the lichen Xanthoria parietina. Our working hypothesis was that parietin content and hydration of the thalli may play a role in the modulation of the effects of O3 exposure. Four batches of X. parietina samples, dry and wet, with (P+) and without (Pâ\u88\u92) parietin, were fumigated for 1 h with 3 ppm O3. The effects of O3 were assessed immediately after the fumigation and after one week of recovery under controlled conditions. O3 fumigation caused physiological and ultrastructural impairment both to the photobiont and the mycobiont, irrespective if samples were fumigated wet or dry, and P+ or Pâ\u88\u92. However, one week after fumigation, a recovery was observed in P+ samples for the photobiont and in dry samples for the mycobiont. We suggest that the hydration state may play a major role in determining the severity of the damage, while the presence of parietin may promote the recovery. Our results provide physiological and ultrastructural basis to explain the ecological insensitivity of lichens to high environmental levels of ozone occurring during dry Mediterranean summers

The extremo-?±-carbonic anhydrase (CA) from Sulfurihydrogenibium azorense the fastest CA known is highly activated by amino acids and amines

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Cloning, expression and purification of the α-carbonic anhydrase from the mantle of the Mediterranean mussel, Mytilus galloprovincialis

We cloned, expressed, purified, and determined the kinetic constants of the recombinant α-carbonic anhydrase (rec-MgaCA) identified in the mantle tissue of the bivalve Mediterranean mussel, Mytilus galloprovincialis. In metazoans, the α-CA family is largely represented and plays a pivotal role in the deposition of calcium carbonate biominerals. Our results demonstrated that rec-MgaCA was a monomer with an apparent molecular weight of about 32 kDa. Moreover, the determined kinetic parameters for the CO2 hydration reaction were kcat =  4.2 × 105 s−1 and kcat/Km of 3.5 × 107 M−1 ×s−1. Curiously, the rec-MgaCA showed a very similar kinetic and acetazolamide inhibition features when compared to those of the native enzyme (MgaCA), which has a molecular weight of 50 kDa. Analysing the SDS-PAGE, the protonography, and the kinetic analysis performed on the native and recombinant enzyme, we hypothesised that probably the native MgaCA is a multidomain protein with a single CA domain at the N-terminus of the protein. This hypothesis is corroborated by the existence in mollusks of multidomain proteins with a hydratase activity. Among these proteins, nacrein is an example of α-CA multidomain proteins characterised by a single CA domain at the N-terminus part of the entire protein