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

Robert E. Martinez, Bruce E. Bowler

Research output: Contribution to journalArticlepeer-review

Abstract

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 pKa 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.

Original languageEnglish
Pages (from-to)6751-6758
Number of pages8
JournalJournal of the American Chemical Society
Volume126
Issue number21
DOIs
StatePublished - Jun 2 2004

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