Detection of a geminate photoproduct of bovine cytochrome c oxidase by time-resolved serial femtosecond crystallography.

ABSTRACT: Cytochrome c oxidase (C c O) is a large membrane-bound hemeprotein that catalyzes the reduction of dioxygen to water. Unlike classical dioxygen binding hemeproteins with a heme b group in their active sites, C c O has a unique binuclear center (BNC) comprised of a copper atom (Cu _B ) and a heme a ₃ iron, where O ₂ binds and is reduced to water. CO is a versatile O ₂ surrogate in ligand binding and escape reactions. Previous time-resolved spectroscopic studies of the CO complexes of bovine C c O (bC c O) revealed that photolyzing CO from the heme a ₃ iron leads to a metastable intermediate (Cu _B -CO), where CO is bound to Cu _B , before it escapes out of the BN

SUBMITTER: Ishigami I 

PROVIDER: S-EPMC10197551 | biostudies-literature | 2023 May

REPOSITORIES: biostudies-literature