Snapshot of an oxygen intermediate in the catalytic reaction of cytochrome c oxidase.

ABSTRACT: Cytochrome c oxidase (CcO) reduces dioxygen to water and harnesses the chemical energy to drive proton translocation across the inner mitochondrial membrane by an unresolved mechanism. By using time-resolved serial femtosecond crystallography, we identified a key oxygen intermediate of bovine CcO. It is assigned to the P_R-intermediate, which is characterized by specific redox states of the metal centers and a distinct protein conformation. The heme a₃ iron atom is in a ferryl (Fe⁴⁺ = O^2-) configuration, and heme a and Cu_B are oxidized while Cu_A is reduced. A Helix-X segment is poised in an open conformational state; the heme a farnesyl sidechain is H-bonded to S382, and loop-I-II ado

SUBMITTER: Ishigami I 

PROVIDER: S-EPMC6397517 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature