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Detection of a Geminate Photoproduct of Bovine Cytochrome cOxidase by Time-Resolved Serial Femtosecond Crystallography
- Source :
- Journal of the American Chemical Society; October 2023, Vol. 145 Issue: 41 p22305-22309, 5p
- Publication Year :
- 2023
-
Abstract
- Cytochrome coxidase (CcO) is a large membrane-bound hemeprotein that catalyzes the reduction of dioxygen to water. Unlike classical dioxygen binding hemeproteins with a heme bgroup in their active sites, CcO has a unique binuclear center (BNC) composed of a copper atom (CuB) and a heme a3iron, where O2binds and is reduced to water. CO is a versatile O2surrogate 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 a3iron leads to a metastable intermediate (CuB-CO), where CO is bound to CuB, before it escapes out of the BNC. Here, with a pump-probe based time-resolved serial femtosecond X-ray crystallography, we detected a geminate photoproduct of the bCcO–CO complex, where CO is dissociated from the heme a3iron and moved to a temporary binding site midway between the CuBand the heme a3iron, while the locations of the two metal centers and the conformation of Helix-X, housing the proximal histidine ligand of the heme a3iron, remain in the CO complex state. This new structure, combined with other reported structures of bCcO, allows for a clearer definition of the ligand dissociation trajectory as well as the associated protein dynamics.
Details
- Language :
- English
- ISSN :
- 00027863 and 15205126
- Volume :
- 145
- Issue :
- 41
- Database :
- Supplemental Index
- Journal :
- Journal of the American Chemical Society
- Publication Type :
- Periodical
- Accession number :
- ejs63871411
- Full Text :
- https://doi.org/10.1021/jacs.3c07803