Contributions to cytochrome c inner- and outer-sphere reorganization energy.

ABSTRACT: Cytochromes c are small water-soluble proteins that catalyze electron transfer in metabolism and energy conversion processes. Hydrogenobacter thermophilus cytochrome c ₅₅₂ presents a curious case in displaying fluxionality of its heme axial methionine ligand; this behavior is altered by single point mutation of the Q64 residue to N64 or V64, which fixes the ligand in a single configuration. The reorganization energy (λ) of these cytochrome c ₅₅₂ variants is experimentally determined using a combination of rotating disc electrochemistry, chronoamperometry and cyclic voltammetry. The differences between the λ determined from these complementary techniques helps to deconvolute the contribution of the active site and its im

SUBMITTER: Chattopadhyay S 

PROVIDER: S-EPMC8442690 | biostudies-literature | 2021 Sep

REPOSITORIES: biostudies-literature