RESUMO
Remarkable increases in enzyme catalytic stability resulting from addition of charged water-soluble polymers have recently been reported, suggesting that use of these polymers may be an attractive general strategy for enzyme stabilization. To test the proposed hypothesis that coulombic forces between water-soluble polymers and enzymes are primarily responsible for enzyme stabilization, we examined the catalytic stability and activity of two enzymes in the presence of polymers differing in net charge. All polymers tested increased enzyme lifetimes, regardless of their net charge, suggesting that stabilization of these enzymes by water-soluble polymers is not solely dependent on simple electrostatic interactions between the polymers and enzymes.
Assuntos
Resinas Acrílicas/farmacologia , Álcool Desidrogenase/metabolismo , Estabilidade Enzimática/efeitos dos fármacos , Polietilenoimina/farmacologia , Saccharomyces cerevisiae/enzimologia , Subtilisinas/metabolismo , Álcool Desidrogenase/efeitos dos fármacos , Solubilidade , Água/químicaRESUMO
We have studied the photochemical reduction of uranyl to generate UO2 without hydrogen reduction. Formate and oxalate were examined as potential reductants that only lead to CO2 production as a side product. Despite the similar nature of the two reductants, the mechanism for quenching the uranyl excited-state changes drastically and leads to dramatically different chemistry at low pH. Oxalate quenches by unimolecular electron transfer and formate quenches by H-atom abstraction. Because of the change in mechanism, photochemical reduction of uranyl with formate works with high efficiency at low pH while photolysis in the presence of oxalate leads to the generation of CO and no net uranyl reduction. Photochemical reduction of uranyl with formate at low pH leads to U(IV) in solution that can then be precipitated as UO2 by simply raising the pH with yields as high as 99.992%.