ArticleProceedings of the National Academy of Sciences of the United States of America2020
Neutron crystallography of copper amine oxidase reveals keto/enolate interconversion of the quinone cofactor and unusual proton sharing.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 14 citations in OpenAlex.
- Real-time capture of domain movements during copper amine oxidase catalysis by mix-and-inject serial crystallography.Nature communications · 2025Article
- Molecular mechanism of a large conformational change of the quinone cofactor in the semiquinone intermediate of bacterial copper amine oxidase.Chemical science · 2022Article
- Re-evaluation of protein neutron crystallography with and without X-ray/neutron joint refinement.IUCrJ · 2022Article
- Current status of neutron crystallography in structural biology.Biophysics and physicobiology · 2022Article
- Metalloprotein catalysis: structural and mechanistic insights into oxidoreductases from neutron protein crystallography.Acta crystallographica. Section D, Structural biology · 2021Review
- Microcrystal preparation for serial femtosecond X-ray crystallography of bacterial copper amine oxidase.Acta crystallographica. Section F, Structural biology communications · 2021Article
- Unique protonation states of aspartate and topaquinone in the active site of copper amine oxidase.RSC advances · 2020Article
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17 authors at 7 institutions in 1 country.
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Abstract
Recent advances in neutron crystallographic studies have provided structural bases for quantum behaviors of protons observed in enzymatic reactions. Thus, we resolved the neutron crystal structure of a bacterial copper (Cu) amine oxidase (CAO), which contains a prosthetic Cu ion and a protein-derived redox cofactor, topa quinone (TPQ). We solved hitherto unknown structures of the active site, including a keto/enolate equilibrium of the cofactor with a nonplanar quinone ring, unusual proton sharing between the cofactor and the catalytic base, and metal-induced deprotonation of a histidine residue that coordinates to the Cu. Our findings show a refined active-site structure that gives detailed information on the protonation state of dissociable groups, such as the quinone cofactor, which are critical for catalytic reactions.
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