PMID: 43839Jan 1, 1979

Hydrogen-tritium exchange titration of the histidine residues in bovine heart cytochrome c and analysis of their microenvironment

International Journal of Peptide and Protein Research


Microenvironments of the three histidine residues located at the positions 18, 26, and 33 from the amino terminus in bovine heart cytochrome c were analysed in solution by the hydrogen-tritium exchange titration method, which has been developed in this laboratory. Histidine-18, which is liganded to the heme iron, and histidine-26 did not incorporate tritium in native state, indicating that the two are located in solvent inaccessible hydrophobic regions. Histidine-33 was labeled with tritium to an appreciable extent and seemed to be partially buried in the molecule. The pKa value estimated for histidine-33 was 6.1 at 37 degrees by the tritium exchange titration, suggesting that the residue interacts very weakly with a neighboring cationic group. These results seem to be compatible with the tertiary structure of the protein deduced from the X-ray crystallographic analysis.


Oct 29, 1982·Molecular and Cellular Biochemistry·C WoodwardE Tüchsen

Related Concepts

Cytochrome c Group
Bos indicus
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