The unfolding of the cytochromes c in methanol and acid.
The cytochromes c are a family of hemoproteins that share a number of structural features: a thioether linkage between the protein and the heme, histidine and methionine as the fifth and sixth iron ligands, and a tertiary structure known as the "cytochrome fold." These proteins follow a common mechanism of equilibrium unfolding in methanol and acid, differing only in their reactivity to the denaturing conditions. The reduced cytochromes c exhibit an increased conformational stability which is consistent with the presence of a strengthened iron-methionine linkage in the reduced state.
D000818:Animals; D003574:Cytochrome c Group; D006418:Heme; D006736:Horses; D006863:Hydrogen-Ion Concentration; D007501:Iron; D000432:Methanol; D009206:Myocardium / Q000201:enzymology; D009994:Osmolar Concentration; D011487:Protein Conformation; D011489:Protein Denaturation; D013053:Spectrophotometry
D003574:Cytochrome c Group; D006418:Heme; D007501:Iron; D000432:Methanol