Báo cáo khoa học: Binding of ligands originates small perturbations on the microscopic thermodynamic properties of a multicentre redox protein
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NMR and visible spectroscopy coupled to redox measurements were usedto determine the equilibrium thermodynamic properties of the four haemsin cytochrome c3under conditions in which the protein was bound to lig-ands, the small anion phosphate and the protein rubredoxin with the ironin the active site replaced by zinc. Comparison of these results with datafor the isolated cytochrome shows that binding of ligands causes only smallchanges in the reduction potentials of the haems and their pairwise inter-actions, and also that the redox-sensitive acid–base centre responsible forthe redox–Bohr effect is essentially unaffected. ...
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Báo cáo khoa học: Binding of ligands originates small perturbations on the microscopic thermodynamic properties of a multicentre redox protein
Nội dung trích xuất từ tài liệu:
Báo cáo khoa học: Binding of ligands originates small perturbations on the microscopic thermodynamic properties of a multicentre redox protein
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