Dendrimer-Encapsulated Pt Nanoparticles: An Artificial Enzyme for Hydrogen Production
Source abstract
Abstract
Two series of dendrimer encapsulated Pt nanoparticles (DENPt) were created by using sixth generation poly(amidoamine) (PAMAM) dendrimers terminated with different numbers of hydroxyl groups (s-G6-OH and t-G6-OH) to mimic hydrogenases. Pt nanoparticles act as the active site to generate H 2 by reducing H +, and dendrimers provide cavities to maintain the integrity of small Pt nanoparticles and prevent agglomeration. The artificial hydrogenases (t-G6-OH/Pt x and s-G6-OH/Pt x ) were successfully applied to a light-induced hydrogen production system with Pt-tppa +, ethyl viologen, and TEOA as photosensitizer, electron relay, and sacrificial reagent, respectively, exhibiting excellent stability and efficient catalytic activity. No passivation effect is caused by the periphery hydroxyl groups of dendrimers. The optimal size of the Pt clusters consists of 200 Pt atoms, and the most adapted pH value is 9 to gain the highest catalytic efficiency in the applied hydrogen production system. This study provides a new strategy for developing artificial hydrogenases by using dendritic architectures.
Source: openalex_inverted_index · Quality: baseline
Research context
OpenAlex topics: Advanced Photocatalysis Techniques · Electrocatalysts for Energy Conversion · Metalloenzymes and iron-sulfur proteins
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
Affiliations
Key Laboratory of Photochemical Conversion and Optoelectronic Materials, Technical Institute of Physics and Chemistry, Chinese Academy of Sciences, Beijing 100190, People's Republic of China
Beijing National Laboratory for Molecular Sciences (BNLMS), Key laboratory of Photochemistry, Institute of Chemistry, Chinese Academy of Sciences, Beijing 100190, People's Republic of China
References (41)
Show source-provided references
1. Barber J. · Chem. Soc. Rev. · 2009 · 38 · 18510.1039/B802262N ↗
2. Lubner C. E. · Biochemistry · 2010 · 49 · 40410.1021/bi901704v ↗
3. Kudo A. · Chem. Soc. Rev. · 2009 · 38 · 25310.1039/B800489G ↗
4. Esswein M. J. · Chem. Rev. · 2007 · 107 · 402210.1021/cr050193e ↗
5. Magnuson A. · Acc. Chem. Res. · 2009 · 42 · 189910.1021/ar900127h ↗
6. Dempsey J. L. · Acc. Chem. Res. · 2009 · 42 · 199510.1021/ar900253e ↗
7. Frey M. · ChemBioChem · 2002 · 3 · 15310.1002/1439-7633(20020301)3:2/3<153::AID-CBIC153>3.0.CO;2-B ↗
8. Happe T. · Eur. J. Biochem. · 1993 · 214 · 47510.1111/j.1432-1033.1993.tb17944.x ↗
9. Happe T. · Eur. J. Biochem. · 1994 · 222 · 76910.1111/j.1432-1033.1994.tb18923.x ↗
10. Allakhverdiev S. I. · Photochem. Photobiol. Sci. · 2009 · 8 · 13710.1039/b823060a ↗
11. LaVan D. A. · Proc. Natl. Acad. Sci. U.S.A. · 2006 · 103 · 525110.1073/pnas.0506694103 ↗
12. Ott S. · Angew. Chem., Int. Ed. · 2004 · 43 · 100610.1002/anie.200353190 ↗
13. Sun L. C. · Coord. Chem. Rev. · 2005 · 249 · 165310.1016/j.ccr.2005.01.013 ↗
14. Markovic N. M. · J. Phys. Chem. B · 1997 · 101 · 540510.1021/jp970930d ↗
15. Esposito D. V. · Angew. Chem., Int. Ed. · 2010 · 49 · 985910.1002/anie.201004718 ↗
16. Harriman A. · J. Chem. Soc. Chem. Commun. · 1990 · 2410.1039/C39900000024 ↗
17. Yonezawa T. · J. Mol. Catal. · 1993 · 83 · 16710.1016/0304-5102(93)87017-3 ↗
18. Persaud L. · J. Am. Chem. Soc. · 1987 · 109 · 730910.1021/ja00258a011 ↗
19. Varpness Z. · Nano Lett. · 2005 · 5 · 230610.1021/nl0517619 ↗
20. Balogh L. · J. Am. Chem. Soc. · 1998 · 120 · 735510.1021/ja980861w ↗
21. Esumi K. · Langmuir · 1998 · 14 · 315710.1021/la980162x ↗
22. Zhao M. Q. · J. Am. Chem. Soc. · 1998 · 120 · 487710.1021/ja980438n ↗
23. Zhao M. Q. · Angew. Chem., Int. Ed. · 1999 · 38 · 36410.1002/(SICI)1521-3773(19990201)38:3<364::AID-ANIE364>3.0.CO;2-L ↗
24. Crooks R. M. · Acc. Chem. Res. · 2001 · 34 · 18110.1021/ar000110a ↗
25. Niu Y. H. · Chem. Mater. · 2003 · 15 · 346310.1021/cm034172h ↗
26. Chandler B. D. · Catal. Today · 2007 · 122 · 37010.1016/j.cattod.2007.01.047 ↗
27. Wilson O. M. · J. Am. Chem. Soc. · 2005 · 127 · 101510.1021/ja045224m ↗
28. Gu Y. L. · J. Power Sources · 2010 · 195 · 42510.1016/j.jpowsour.2009.07.044 ↗
29. Yang Q. Z. · Inorg. Chem. · 2002 · 41 · 565310.1021/ic025580a ↗
30. Tomalia D. A. · Macromolecules · 1986 · 19 · 246610.1021/ma00163a029 ↗
31. Tomalia D. A. · J. Am. Chem. Soc. · 1987 · 109 · 160110.1021/ja00239a068 ↗
32. Tomalia D. A. · Top. Curr. Chem. · 1993 · 165 · 19310.1007/BFb0111285 ↗
33. Knecht M. R. · Chem. Mater. · 2008 · 20 · 521810.1021/cm8004198 ↗
34. Miyake M. · J. Phys. Chem. B · 1999 · 103 · 3818
35. Ye H. · Langmuir · 2007 · 23 · 1190110.1021/la702297m ↗
36. Maeda H. · Chem. Pharm. Bull. · 1994 · 42 · 187010.1248/cpb.42.1870 ↗
37. Maeda H. · Anal. Sci. · 2000 · 16 · 29310.2116/analsci.16.293 ↗
38. Koca A. · Electroanalysis · 2010 · 22 · 162310.1002/elan.200900545 ↗
39. Nyokong T. · Polyhedron · 2007 · 26 · 535510.1016/j.poly.2007.08.007 ↗
40. Kaneko M. · J. Mol. Catal., A: Chem. · 1999 · 145 · 24510.1016/S1381-1169(99)00013-8 ↗
41. Greenbaum E. · J. Phys. Chem. · 1988 · 92 · 457110.1021/j100327a001 ↗