Modulation of the alkaline transition in cytochrome c and cytochrome c-T by full or specific partial acetimidylation

Acetimidylated horse cytochrome c and related derivatives exhibit more or less marked changes, both upscale and downscale, in apparent pK of the alkaline transition. This transition occurs when the normal methionine-80 residue is replaced at the sixth haem co-ordination position by another strong-fi...

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Bibliographic Details
Published in:Biochemical journal 1984-02, Vol.217 (3), p.601-604
Main Author: Wallace, C J
Format: Article
Language:English
Subjects:
Alkalies
Chemical Phenomena
Chemistry
Cytochrome c Group - analogs & derivatives
Cytochromes c
Ligands
Osmolar Concentration
Peptide Fragments
Spectrophotometry
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Summary:Acetimidylated horse cytochrome c and related derivatives exhibit more or less marked changes, both upscale and downscale, in apparent pK of the alkaline transition. This transition occurs when the normal methionine-80 residue is replaced at the sixth haem co-ordination position by another strong-field ligand. Analysis of the relationship between structural change and pK shift in these derivatives supports the view that the replacement ligand is a lysine residue, probably 72 or 79, and contradicts an alternative hypothesis. The results add further detail to a comprehensive view of the mechanism of this isomerization.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj2170601