Journal
ACS CATALYSIS
Volume 13, Issue 7, Pages 4134-4141Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acscatal.2c059464134
Keywords
artificial metalloenzyme; photocatalysis; energy transfer reaction; protein labeling; singlet oxygen
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By incorporating a DNA photo-switch metal complex, researchers have developed a photo-driven artificial metalloenzyme. This artificial metalloenzyme can switch between two potential competing photocatalytic reaction pathways by the photo-switch complex or when working together. This finding has been utilized for selective protein labeling.
While photocatalysts have been recognized as powerful and environmentally friendly catalysts, harnessing their reactivity still remains challenging. On account of the distinctive reaction compartment that their protein scaffolds provide for the incorporated metal complex, artificial metalloenzymes (ArMs) can improve catalytic reaction rates and stereochemical selectivity. In the present study, we have developed a photo-driven ArM by incorporating a DNA photo-switch metal complex, [Ru-(bpy)2dppz]2+ (1), into an apo-form riboflavin-binding protein (RFBP). We report that two potentially competing photocatalytic reaction pathways, i.e., a photoredox reaction and an energy transfer reaction, can be switched by 1 alone and by the ArM. This reaction switching was exploited in selective protein labeling; 1 alone preferentially promotes tyrosine modification, while the ArM promotes histidine modification. The present study thus opens the door for the potential use of ArMs to control the reactivity of photocatalysts.
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