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

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 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.

Citations

Jul 14, 2009·Journal of Bioenergetics and Biomembranes·Tianlei YingXiangshi Tan
Apr 10, 2010·Chemical Communications : Chem Comm·Tianlei YingZhong-Xian Huang
Mar 22, 2013·Protein Engineering, Design & Selection : PEDS·Tianlei YingZhong-Xian Huang
Feb 12, 2014·Metallomics : Integrated Biometal Science·Antonio RanieriMarco Sola
Apr 23, 2016·Biochemistry·Levi J McClelland, Bruce E Bowler
Jan 19, 2016·Journal of Inorganic Biochemistry·Matthew E GoldesBruce E Bowler
Jun 16, 2007·Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry·Gianantonio BattistuzziSachiko Yanagisawa
May 8, 2015·Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry·Levi J McClellandBruce E Bowler
Dec 14, 2004·Yeast

Related Concepts

CYC1 protein, S cerevisiae
Histidine
Hydrogen-Ion Concentration
Alloenzymes
Lysine Hydrochloride
Pedameth
Protein Conformation
Protons
Saccharomyces cerevisiae
Spectrophotometry

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