Cooperative catalysis by a single-atom enzyme-metal complex

Xiaoyang Li, Yufei Cao, Kai Luo, Lin Zhang (), Yunxiu Bai, Jiarong Xiong, Richard N. Zare () and Jun Ge ()
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Xiaoyang Li: Tsinghua University
Yufei Cao: Tsinghua University
Kai Luo: Fudan University
Lin Zhang: Tianjin University
Yunxiu Bai: Tsinghua University
Jiarong Xiong: Tsinghua University
Richard N. Zare: Fudan University
Jun Ge: Tsinghua University

Nature Communications, 2022, vol. 13, issue 1, 1-8

Abstract: 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−1), exceeding that of the traditional catalyst Pd(OAc)2 by a factor of 300 under ambient conditions.

Date: 2022
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DOI: 10.1038/s41467-022-29900-6

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