Proton-mediated dynamics of the alkaline conformational transition of yeast iso-1-cytochrome c

Journal of the American Chemical Society
Robert E Martinez, Bruce E Bowler


The kinetics of the alkaline conformational transition of a Lys 73-->His variant of iso-1-cytochrome c have been investigated using pH jump stopped-flow methods to probe the nature of the ionizable "trigger" group for this conformational change. This mutation moves the pK(a) of the ligand replacing Met 80 from about 10.5 to approximately 6.6 and has unmasked two other ionizable groups, besides the ligand replacing Met 80, that modulate the kinetics of this process. The results are discussed in terms of the impact of ionization equilibria on protein folding mechanisms.


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Related Concepts

CYC1 protein, S cerevisiae
Hydrogen-Ion Concentration
Lysine Hydrochloride
Protein Conformation
Saccharomyces cerevisiae

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