Incorporating ATP into biomimetic catalysts for realizing exceptional enzymatic performance over a broad temperature range
Source abstract
Abstract
There has been great interest in the development of artificial inorganic nanomaterials that mimic natural peroxidases. Unfortunately, these nanomaterials usually possess relatively low catalytic activity and are generally considered to work effectively only within a narrow temperature range (for example, they are inactive at high temperatures). Intriguingly, adenosine triphosphate (ATP) is not only the ubiquitous energy currency of life, it is also known to form charge transfer complexes with aromatic molecules and to participate in free radical redox chemistry. Inspired by its unique properties, for the first time, we reveal a novel catalytic role for ATP and show that ATP is an ideal boosting agent for markedly improving the catalytic activity of a peroxidase mimic over a broad temperature range and, more significantly, making it possible to achieve exceptionally efficient high-temperature catalytic reactions. These observations pave the way for identifying highly effective modulators that promote the overall performance of artificial enzymes. Jinsong Ren, Xiaogang Qu and colleagues at the Changchun Institute of Applied Chemistry in China have shown that adenosine triphosphate (ATP), a key biochemical molecule in metabolism, greatly enhances the activity of ‘nanozymes’ — stable enzyme-mimicking inorganic catalysts. Many researchers are trying to develop nanozymes for industrial and environmental applications, since enzymes themselves are fragile, expensive to isolate and only active within a narrow temperature range. Ren, Qu and colleagues investigated nanozymes composed of gold and silica that act like a peroxidase enzyme, catalyzing electron-transfer ‘redox’ reactions. When they added ATP, the catalytic efficiency of the nanozymes dramatically increased. The researchers also found that the nanozymes function over a broad temperature range including high temperatures suited to industrial applications. Their work suggests the more general possibility that other simple biochemicals could enhance the potential of inorganic enzyme mimics. ATP can act an ideal boosting agent for markedly improving the peroxidase-like catalytic activity over a broad temperature range.
Source: openalex_inverted_index · Quality: baseline
Research context
OpenAlex topics: Advanced Nanomaterials in Catalysis · Electrochemical sensors and biosensors · Nanocluster Synthesis and Applications
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
References (43)
Show source-provided references
1. Barber, J. Photosynthetic energy conversion: natural and artificial. Chem. Soc. Rev. 38, 185–196 (2009).10.1039/B802262N ↗
2. Breslow, R. Biomimetic chemistry and artificial enzymes: catalysis by design. Acc. Chem. Res. 28, 146–153 (1995).10.1021/ar00051a008 ↗
3. Hult, K. & Berglund, P. Engineered enzymes for improved organic synthesis. Curr. Opin. Biotechnol. 14, 395–400 (2003).10.1016/S0958-1669(03)00095-8 ↗
4. Gao, L., Zhuang, J., Nie, L., Zhang, J., Zhang, Y., Gu, N., Wang, T., Feng, J., Yang, D., Perrett, S. & Yan, X. Intrinsic peroxidase-like activity of ferromagnetic nanoparticles. Nat. Nanotechnol. 2, 577–583 (2007).10.1038/nnano.2007.260 ↗
5. Xie, J., Zhang, X., Wang, H., Zheng, H. & Huang, Y. Analytical and environmental applications of nanoparticles as enzyme mimetics. TrAC, Trends Anal. Chem. 39, 114–129 (2012).10.1016/j.trac.2012.03.021 ↗
6. Asati, A., Santra, S., Kaittanis, C., Nath, S. & Perez, J. M. Oxidase-like activity of polymer-coated cerium oxide nanoparticles. Angew. Chem. Int. Ed. 8, 2308–2312 (2009).10.1002/anie.200805279 ↗
7. Manea, F., Houillon, F. B., Pasquato, L. & Scrimin, P. Nanozymes: gold-nanoparticle-based transphosphorylation catalysts. Angew. Chem. Int. Ed. 43, 6165–6169 (2004).10.1002/anie.200460649 ↗
8. Pengo, P., Polizzi, S., Pasquato, L. & Scrimin, P. Carboxylate−imidazole cooperativity in dipeptide-functionalized gold nanoparticles with esterase-like activity. J. Am. Chem. Soc. 127, 1616–1617 (2005).10.1021/ja043547c ↗
9. Liu, S., Lu, F., Xing, R. & Zhu, J.-J. Structural effects of Fe3O4 nanocrystals on peroxidase-like activity. Chem. Eur. J. 17, 620–625 (2011).10.1002/chem.201001789 ↗
10. Asati, A., Kaittanis, C., Santra, S. & Perez, J. M. pH-Tunable oxidase-like activity of cerium oxide nanoparticles achieving sensitive fluorigenic detection of cancer biomarkers at neutral pH. Anal. Chem. 83, 2547–2553 (2011).10.1021/ac102826k ↗
11. Heckert, E. G., Karakoti, A. S., Seal, S. & Self, W. T. The role of cerium redox state in the SOD mimetic activity of nanoceria. Biomaterials 29, 2705–2709 (2008).10.1016/j.biomaterials.2008.03.014 ↗
12. Singh, S., Dosani, T., Karakoti, A. S., Kumar, A., Seal, S. & Self, W. T. A phosphate-dependent shift in redox state of cerium oxide nanoparticles and its effects on catalytic properties. Biomaterials 32, 6745–6753 (2011).10.1016/j.biomaterials.2011.05.073 ↗
13. André, R., Natálio, F., Humanes, M., Leppin, J., Heinze, K., Wever, R., Schröder, H. C., Müller, W. E. G. & Tremel, W. V2O5 Nanowires with an intrinsic peroxidase-like activity. Adv. Funct. Mater. 21, 501–509 (2011).10.1002/adfm.201001302 ↗
14. Natalio, F., André, R., Hartog, A. F., Stoll, B., Jochum, K. P., Wever, R. & Tremel, W. Vanadium pentoxide nanoparticles mimic vanadium haloperoxidases and thwart biofilm formation. Nat. Nanotechnol. 7, 530–535 (2012).10.1038/nnano.2012.91 ↗
15. Comotti, M., Della Pina, C., Matarrese, R. & Rossi, M. The catalytic activity of “naked” gold particles. Angew. Chem. Int. Ed. 43, 5812–5815 (2004).10.1002/anie.200460446 ↗
16. Comotti, M., Della Pina, C., Falletta, E. & Rossi, M. Aerobic oxidation of glucose with gold catalyst: hydrogen peroxide as intermediate and reagent. Adv. Synth. Catal. 348, 313–316 (2006).10.1002/adsc.200505389 ↗
17. Luo, W., Zhu, C., Su, S., Li, D., He, Y., Huang, Q. & Fan, C. Self-catalyzed, self-limiting growth of glucose oxidase-mimicking gold nanoparticles. ACS Nano 4, 7451–7458 (2010).10.1021/nn102592h ↗
18. Zheng, X., Liu, Q., Jing, C., Li, Y., Li, D., Luo, W., Wen, Y., He, Y., Huang, Q., Long, Y. T. & Fan, C. Catalytic gold nanoparticles for nanoplasmonic detection of DNA hybridization. Angew. Chem. Int. Ed. 50, 11994–11998 (2011).10.1002/anie.201105121 ↗
19. Sun, X., Guo, S., Chung, C.-S., Zhu, W. & Sun, S. A sensitive H2O2 assay based on dumbbell-like PtPd-Fe3O4 nanoparticles. Adv. Mater. 25, 132–136 (2013).10.1002/adma.201203218 ↗
20. Sun, X., Guo, S., Liu, Y. & Sun, S. Dumbbell-like PtPd–Fe3O4 nanoparticles for enhanced electrochemical detection of H2O2. Nano Lett. 12, 4859–4863 (2012).10.1021/nl302358e ↗
21. Song, Y. J., Wang, X., Zhao, C., Qu, K., Ren, J. & Qu, X. Label-free colorimetric detection of single nucleotide polymorphism by using single-walled carbon nanotube intrinsic peroxidase-like activity. Chem.-Eur. J 16, 3617–3621 (2010).10.1002/chem.200902643 ↗
22. Cui, R., Han, Z. & Zhu, J.-J. Helical carbon nanotubes: intrinsic peroxidase catalytic activity and its application for biocatalysis and biosensing. Chem. Eur. J. 17, 9377–9384 (2011).10.1002/chem.201100478 ↗
23. Song, Y., Qu, K., Zhao, C., Ren, J. & Qu, X. Graphene oxide: intrinsic peroxidase catalytic activity and its application to glucose detection. Adv. Mater. 22, 2206–2210 (2010).10.1002/adma.200903783 ↗
24. Xue, T., Jiang, S., Qu, Y., Su, Q., Cheng, R., Dubin, S., Chiu, C. Y., Kaner, R., Huang, Y. & Duan, X. Graphene-supported hemin as a highly active biomimetic oxidation catalyst. Angew. Chem. Int. Ed. 51, 3822–3825 (2012).10.1002/anie.201108400 ↗
25. Dong, Z., Luo, Q. & Liu, J. Artificial enzymes based on supramolecular scaffolds. Chem. Soc. Rev. 41, 7890–7908 (2012).10.1039/c2cs35207a ↗
26. Lin, Y., Ren, J. & Qu, X. Catalytically active nanomaterials: a promising candidate for artificial enzymes. Acc. Chem. Res. 47, 1097–1105 (2014).10.1021/ar400250z ↗
27. Kotov, N. A. Inorganic nanoparticles as protein mimics. Science 330, 188–189 (2010).10.1126/science.1190094 ↗
28. Lin, Y., Zhao, A., Tao, Y., Ren, J. & Qu, X. Ionic liquid as an efficient modulator on artificial enzyme system: toward the realization of high-temperature catalytic reactions. J. Am. Chem. Soc. 135, 4207–4210 (2013).10.1021/ja400280f ↗
29. Kalckar, H. M. The nature of energetic coupling in biological syntheses. Chem. Rev. 28, 71–178 (1941).10.1021/cr60089a002 ↗
30. Huh, S., Wiench, J. W., Yoo, J. C., Pruski, M. & Lin, V. S. Y. Organic functionalization and morphology control of mesoporous silicas via a co-condensation synthesis method. Chem. Mater. 15, 4247–4256 (2003).10.1021/cm0210041 ↗
31. Kim, M.-H., Na, H. K., Kim, Y. K., Ryoo, S. R., Cho, H. S., Lee, K. E., Jeon, H., Ryoo, R. & Min, D. H. Facile synthesis of monodispersed mesoporous silica nanoparticles with ultralarge pores and their application in gene delivery. ACS Nano 5, 3568–3576 (2011).10.1021/nn103130q ↗
32. Angelos, S., Khashab, N. M., Yang, Y. W., Trabolsi, A., Khatib, H. A., Stoddart, J. F. & Zink, J. I. pH clock-operated mechanized nanoparticles. J. Am. Chem. Soc. 131, 12912–12914 (2009).10.1021/ja9010157 ↗
33. Lin, Y., Li, Z., Chen, Z., Ren, J. & Qu, X. Mesoporous silica-encapsulated gold nanoparticles as artificial enzymes for self-activated cascade catalysis. Biomaterials 34, 2600–2610 (2013).10.1016/j.biomaterials.2013.01.007 ↗
34. Motomizu, S., Wakimoto, T. & Toei, K. Spectrophotometric determination of phosphate in river waters with molybdate and malachite green. Analyst 108, 361–367 (1983).10.1039/AN9830800361 ↗
35. Stefan, L., Denat, F. & Monchaud, D. Insights into how nucleotide supplements enhance the peroxidase-mimicking DNAzyme activity of the G-quadruplex/hemin system. Nucleic Acids Res. 40, 8759–8772 (2012).10.1093/nar/gks581 ↗
36. Blocker, R. & Roth, J. S. The reduction of uridine 5'-diphosphate and uridine 5'-triphosphate in some transplantable rat hepatomas. Cancer Res. 37, 1923–1928 (1977).
37. Jordan, A. & Reichard, P. Ribonucleotide reductases. Annu. Rev. Biochem. 67, 71–98 (1998).10.1146/annurev.biochem.67.1.71 ↗
38. Jordan, A., Torrents, E., Sala, I., Hellman, U., Gibert, I. & Reichard, P. Ribonucleotide reduction in Pseudomonas species: Simultaneous presence of active enzymes from different classes. J. Bacteriol. 181, 3974–3980 (1999).10.1128/JB.181.13.3974-3980.1999 ↗
39. Kong, D.-M., Xu, J. & Shen, H.-X. Positive effects of ATP on G-Quadruplex-Hemin DNAzyme-mediated reactions. Anal. Chem. 82, 6148–6153 (2010).10.1021/ac100940v ↗
40. Pei, H., Zuo, X., Pan, D., Shi, J., Huang, Q. & Fan, C. Scaffolded biosensors with designed DNA nanostructures. NPG Asia Mat. 5, e51 (2013).10.1038/am.2013.22 ↗
41. He, W., Zhou, Y. T., Wamer, W. G., Hu, X., Wu, X., Zheng, Z., Boudreau, M. D. & Yin, J. J. Intrinsic catalytic activity of Au nanoparticles with respect to hydrogen peroxide decomposition and superoxide scavenging. Biomaterials 34, 765–773 (2013).10.1016/j.biomaterials.2012.10.010 ↗
42. Li, T., Dong, S. & Wang, E. G-Quadruplex aptamers with peroxidase-like DNAzyme functions: which is the best and how does it work? Chem. Asian J. 4, 918–922 (2009).10.1002/asia.200900019 ↗
43. Lee, C. & Yoon, J. UV direct photolysis of 2,2‘-azino-bis(3-ethylbenzothiazoline-6-sulfonate) (ABTS) in aqueous solution: Kinetics and mechanism. J. Photochem. Photobiol. 197, 232–238 (2008).10.1016/j.jphotochem.2007.12.030 ↗