Cooperative catalysis by a single-atom enzyme-metal complex.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 35449166.
- Also identified by DOI 10.1038/s41467-022-29900-6 and PMC identifier 9023488.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
Anchoring single metal atoms on enzymes has great potential to generate hybrid catalysts with high activity and selectivity for reactions that cannot be driven by traditional metal catalysts. Herein, we develop a photochemical method to construct a stable single-atom enzyme-metal complex by binding single metal atoms to the carbon radicals generated on an enzyme-polymer conjugate. The metal mass loading of Pd-anchored enzyme is up to 4.0% while maintaining the atomic dispersion of Pd. The cooperative catalysis between lipase-active site and single Pd atom accelerates alkyl-alkyl cross-coupling reaction between 1-bromohexane and B-n-hexyl-9-BBN with high efficiency (TOF is 540 h<sup>-1</sup>), exceeding that of the traditional catalyst Pd(OAc)<sub>2</sub> by a factor of 300 under ambient conditions.
Medical subject headings
- Coordination Complexes
- Metals