Crystal structure of CO-bound cytochrome c oxidase determined by serial femtosecond X-ray crystallography at room temperature
- 11 July 2017
- journal article
- research article
- Published by National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 114 (30) , 8011-8016
Abstract
Significance: A fundamental bioenergetics question is how the redox energy from oxygen reduction in cytochrome c oxidase (C c O) is coupled to proton translocation. Although crystallography has revealed many properties of the enzyme, the coupling mechanism remains elusive, in part due to artifacts caused by X-ray damage from synchrotron radiation. We determined the structure of CO-bound bovine C c O by serial femtosecond X-ray crystallography (SFX) with an X-ray free electron laser, outrunning radiation damage. The SFX structure is compared with the structure obtained with synchrotron radiation in which the Fe–CO bond was cleaved. Our results reveal that ligand binding to heme a 3 triggers an allosteric structural transition that may play a critical role in proton translocation in the C c O family of enzymes.Keywords
Funding Information
- HHS | NIH | National Institute of General Medical Sciences (GM098799)
- HHS | NIH | National Institute of General Medical Sciences (GM115773)
- HHS | NIH | National Institute of General Medical Sciences (GM095583)
- National Science Foundation (CHE-1404929)
- National Science Foundation (ABI-1565180)
- National Science Foundation (STC-1231306)
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