Distal Unfolding of Ferricytochrome c Induced by the F82K Mutation.

ABSTRACT: It is well known that axial coordination of heme iron in mitochondrial cytochrome c has redox-dependent stability. The Met80 heme iron axial ligand in the ferric form of the protein is relatively labile and can be easily replaced by alternative amino acid side chains under non-native conditions induced by alkaline pH, high temperature, or denaturing agents. Here, we showed a redox-dependent destabilization induced in human cytochrome c by substituting Phe82-conserved amino acid and a key actor in cytochrome c intermolecular interactions-with a Lys residue. Introducing a positive charge at position 82 did not significantly affect the structure of ferrous cytochrome c but caused localized unfolding of the distal site in the ferric state. As revealed by ¹H NMR fingerprint, the ferr

SUBMITTER: Lalli D 

PROVIDER: S-EPMC7139943 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature