Journal
JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY A-CHEMISTRY
Volume 406, Issue -, Pages -Publisher
ELSEVIER SCIENCE SA
DOI: 10.1016/j.jphotochem.2020.112926
Keywords
Light-harvesting complex; Chlorophyll-membrane protein; Photoreduction; Photoinduced hydrogen production
Categories
Funding
- JSPS KAKENHI [JP 17KT0146, 17K18013, 18H05160, 20H05097]
- AOARD [FA2386-19-1-4033]
- Grants-in-Aid for Scientific Research [17K18013, 20H05097, 18H05160] Funding Source: KAKEN
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The study found that the monomeric form of LHCII has higher photocatalytic activity compared to the trimer form, as well as more significant fluorescence quenching by methylviologen. In the presence of Pt nanoparticles in a catalytic solution system, photoinduced hydrogen production was observed for the LHCII monomer.
Light-harvesting complex of photosystem II (LHCII) is the most abundant membrane protein-chlorophyll complex in chloroplasts. Here, we evaluated the photocatalytic activity of the native trimer and the enzymatically treated monomer forms of LHCII. Upon white light irradiation using a solar simulator, photocatalytic reduction of methylviologen revealed that the activity of monomeric LHCII was higher than that of the trimer form. Fluorescence of the monomeric LHCII was more significantly quenched by methylviologen than that of the trimer form. In the presence of Pt nanoparticles in a catalytic solution system, photoinduced hydrogen production was observed for the LHCII monomer. The difference in photocatalytic activities of LHCII trimer and monomer are briefly discussed in terms of an interaction between LHCII and methylviologen.
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