Ligand binding to cytochrome c and other related haem proteins and peptides. Part III. Temperature dependence studies

Autor: M.M.M. Saleem, Michael T. Wilson
Rok vydání: 1988
Předmět:
Zdroj: Inorganica Chimica Acta. 153:105-113
ISSN: 0020-1693
Popis: The temperature dependency of ligand binding processes lend support to the proposed mechanisms and the factors affecting ligand binding reported earlier in this series. The free energy contribution from each factor affecting ligand binding was estimated for a number of haem proteins. The structures of the haem proteins used, as conveyed from ligand binding data, are in agreement with the structures of these haem proteins as determined by other methods (e.g. X-ray crystallography, NMR, etc.). Therefore, ligand binding could be used as a facile probe to investigate some of the structural and functional properties of haem proteins. In this respect, it was concluded that the structure of native cytochrome c at pH 10 is similar to the structure of carboxymethyl-Met 80 cytochrome c between pH 7 and 10.
Databáze: OpenAIRE