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|Type:||Artigo de periódico|
|Title:||An Esr Study Of Nitrosyl-aplysia Brasiliana Myoglobin And Nitrosyl Annelidae Glossoscolex Paulistus Erythrocruorin|
|Abstract:||The nitrosyl derivatives of Annelidae Glossoscolex paulistus hemoglobin (an earth worm erythrocruorin (Ec AGp)) and Aplysia brasiliana myoglobin (Mb Apb) are studied using ESR spectroscopy. These two proteins have a quite similar ESR spectra at 100 K, but a different temperature behaviour. The temperature dependence of the nitrosyl Mb Apb spectrum is in good agreement with the Boltzmann distribution. In the case of nitrosyl-Ec AGp, the results are explained by the existence of two types of spectrum in thermodynamic equilibrium, with ΔH = 9.08 kJ/mol, ΔS = 47.15 J/mol and T1 2 = 193 K. There is a great similarity of the nitrosyl-Ec AGp spectra with those reported for elephant myoglobin, suggesting teh presence of the same heme environment with a glutamine residue in the distal site. The pH dependence of the spectrum of nitrosyl-Mb Apb shows that the affinity for nitrosyl binding is higher at high pH (7.3) than at low pH (4.6). The ESR parameters are the same for these two pH values. © 1988.|
|Appears in Collections:||Unicamp - Artigos e Outros Documentos|
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