Dramatic stabilization of ferricytochrome c upon reduction.
By combining measurements of the free energy of denaturation of the C102T variant of Saccharomyces cerevisiae iso-1-ferricytochrome c with determination of the formal potentials for the native and chemically-denatured states we have determined the free energy of denaturation of the ferro form of the protein. We report that the simplest of all chemical modifications, addition of an electron, increases the stability of ferricytochrome c by approximately 10 kcal mol-1 at 300 K, pH 4.6. This makes reduced cytochrome c one of the most stable proteins yet investigated.
Hilgen-Willis
S
S
Department of Chemistry, University of North Carolina, Chapel Hill.
Bowden
E F
EF
Pielak
G J
GJ
D003574:Cytochrome c Group / Q000737:chemistry*; D004795:Enzyme Stability; D010084:Oxidation-Reduction; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013816:Thermodynamics
D003574:Cytochrome c Group