Controlling outer-sphere solvent reorganization energy to turn on or off the function of artificial metalloenzymes

Divyansh Prakash, Suchitra Mitra, Simran Sony, Morgan Murphy, Babak Andi, Landon Ashley, Pallavi Prasad and Saumen Chakraborty ()
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Divyansh Prakash: University of Mississippi
Suchitra Mitra: University of Mississippi
Simran Sony: University of Mississippi
Morgan Murphy: University of Mississippi
Babak Andi: Brookhaven National Laboratory
Landon Ashley: University of Mississippi
Pallavi Prasad: University of Mississippi
Saumen Chakraborty: University of Mississippi

Nature Communications, 2025, vol. 16, issue 1, 1-13

Abstract: Abstract Metalloenzymes play essential roles in biology. However, unraveling how outer-sphere interactions can be predictably controlled to influence their functions remains a significant challenge. Inspired by Cu enzymes, we demonstrate how variations in the primary, secondary, and outer coordination-sphere interactions of de novo designed artificial copper proteins (ArCuPs) within trimeric (3SCC) and tetrameric (4SCC) self-assemblies—featuring a trigonal Cu(His)3 and a square pyramidal Cu(His)4(OH2) coordination—influence their catalytic and electron transfer properties. While 3SCC electrocatalyzes C-H oxidation, 4SCC does not. CuI-3SCC reacts more rapidly with H2O2 than O2, whereas 4SCC is less active. Electron transfer, reorganization energies, and extended H2O-mediated hydrogen bonding patterns provide insights into the observed reactivity differences. The inactivity of 4SCC is attributed to a significant solvent reorganization energy barrier mediated by a specific His---Glu hydrogen bond. When this hydrogen bond is disrupted, the solvent reorganization energy is reduced, and C-H peroxidation activity is restored.

Date: 2025
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DOI: 10.1038/s41467-025-57904-5

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