Abstract
The self-assembly of tyrosyl bolaamphiphiles is exploited to create a colloidal protein-like host matrix, upon which sacrificial electron-donor molecules associate to create a photosystem II (PSII) mimetic electron-relay system. This system harnesses the tyrosine phenol groups abundant on the surface of the assemblies to mediate photoinduced intermolecular electron transfer. Compared with the l-tyrosine molecules, the tyrosyl bolaamphiphile assembly facilitates electron transfer from the sacrificial electron donor to the oxidized photosensitizer. The enhanced electron relay is likely to be driven by the host function of the assembly associated with the sacrificial electron donor and by the suppression of the oxidative cross-linking of phenoxyl radicals. The tyrosyl bolaamphiphile assembly is advantageous in the construction of a PSII mimetic system with a protein-like nature and displaying biochemical functions.
| Original language | English |
|---|---|
| Pages (from-to) | 643-650 |
| Number of pages | 8 |
| Journal | ChemPhysChem |
| Volume | 19 |
| Issue number | 5 |
| DOIs | |
| Publication status | Published - 2018 Mar 5 |
Bibliographical note
Funding Information:This work supports by the Research Foundation of Korea (NRF) grant funded by the Korean government (MEST) (NRF-2016R1D1A1A09917929 and 2016R1E1A1A01943379) and by the Human Resources Program in Energy Technology of the Korea Institute of Energy Technology Evaluation and Planning (KETEP), which was granted financial resources by the Ministry of Trade, Industry & Energy, Republic of Korea (no. 20154010200810).
Publisher Copyright:
© 2018 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim
All Science Journal Classification (ASJC) codes
- Atomic and Molecular Physics, and Optics
- Physical and Theoretical Chemistry