Detection of a Geminate Photoproduct of Bovine Cytochrome c Oxidase by Time-Resolved Serial Femtosecond Crystallography.

ABSTRACT: Cytochrome c oxidase (CcO) 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, CcO has a unique binuclear center (BNC) composed of a copper atom (Cu_B) and a heme a₃ iron, where O₂ binds and is reduced to water. CO is a versatile O₂ surrogate in ligand binding and escape reactions. Previous time-resolved spectroscopic studies of the CO complexes of bovine CcO (bCcO) revealed that photolyzing CO from the heme a₃ iron leads to a metastable intermediate (Cu_B-CO), where CO is bound to Cu_B, before it escapes out of the BNC. Here, with a pum

SUBMITTER: Ishigami I 

PROVIDER: S-EPMC10814876 | biostudies-literature | 2023 Oct

REPOSITORIES: biostudies-literature