Abstract
Bovine serum albumin (BSA) has a uranyl(VI) binding hotspot where uranium is tightly bound by three carboxylates. Uranyl oxygen is "soaked" into the hydrophobic core of BSA. Isopropyl hydrogen of Val is trapped near UO22+ and upon photoexcitation, C-H bond cleavage is initiated. A unique hydrophobic contact with "yl"-oxygen, as observed here, can be used to induce C-H activation.
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