Modulation of the alkaline transition in cytochrome c and cytochrome c-T by full or specific partial acetimidylation
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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.
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2009 ◽
Vol 37
(4)
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pp. 293-298
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2019 ◽
Vol 122
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pp. 695-704
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2015 ◽
Vol 585
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pp. 52-63
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2000 ◽
pp. 189-204
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