Hydrogen bonding rearrangement by a mitochondrial disease mutation in cytochrome bc₁ perturbs heme b_H redox potential and spin state.

ABSTRACT: Hemes are common elements of biological redox cofactor chains involved in rapid electron transfer. While the redox properties of hemes and the stability of the spin state are recognized as key determinants of their function, understanding the molecular basis of control of these properties is challenging. Here, benefiting from the effects of one mitochondrial disease-related point mutation in cytochrome b, we identify a dual role of hydrogen bonding (H-bond) to the propionate group of heme b_H of cytochrome bc₁, a common component of energy-conserving systems. We found that replacing conserved glycine with serine in the vicinity of heme b_H caused stabilization of this bond, which not only increased the redox potential of the heme b

SUBMITTER: Kuleta P 

PROVIDER: S-EPMC8379992 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature