期刊
ACS CATALYSIS
卷 8, 期 12, 页码 11352-+出版社
AMER CHEMICAL SOC
DOI: 10.1021/acscatal.8b03811
关键词
DNAzyme; G4/hemin complex; G4-based catalyst; G-quartet; proximal nucleobases
资金
- National Natural Science Foundation of China [21503229, 21635005, 21361162002]
- Fundamental Research Funds for the Central Universities [020514380070, 020514380085, 020514380105, 020514380144]
- self-funding projects from State Key Laboratory of Analytical Chemistry for Life Science, Nanjing University [5431ZZXM1711]
- Nanjing University Innovation and Creative Program for PhD candidate [CXCY17-17]
- Agence Nationale de la Recherche [ANR-17-CE17-0010-01]
- European Research Council [H2020-MSCA-IF-2016-750368]
- Universite de Bourgogne (uB)
- Conseil Regional de Bourgogne (CRB)
- European Union [PO FEDER-FSE Bourgogne 2014/2020 programs]
- Czech Science Foundation [GA16-13721S]
- ERDF project SYMBIT [CZ.02.1.01/0.0/0.0/15_003/0000477]
- Recruitment Program for Foreign Experts (1000plan) of China [WQ20163200397]
- Nanjing University [020514912216]
G-quadruplexes (G4s) are versatile catalytic DNAs when combined with hemin. Despite the repertoire of catalytically competent G4/hemin complexes studied so far, little is known about the detailed catalytic mechanism of these biocatalysts. Herein, we have carried out an in-depth analysis of the hemin binding site within the G4/hemin catalysts, providing the porphyrinic cofactor with a controlled nucleotidic environment. We intensively assessed the position-dependent catalytic enhancement in model reactions and found that proximal nucleobases enhance the catalytic ability of the G4/hemin complexes. Our results allow for revisiting the mechanism of the G4/hemin-based catalysis, especially gaining insights into the rate-limiting step, demonstrating how both the G4 core and the proximal nucleotides dA and/or dC concomitantly activate the Compound 0 -> 0* prototropic cleavage of H2O2 to foster Compound 1 formation. These results provide mechanistic clues as to how the properties of G4-based catalysts can be improved to ultimately make them competitive with proteinaceous enzymes.
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