期刊
JOURNAL OF PHYSICAL CHEMISTRY B
卷 123, 期 44, 页码 9312-9320出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.jpcb.9b06293
关键词
-
资金
- European Union's Horizon 2020 research and innovation programme under the Marie Sklodowska-Curie grant [675006]
- Czech Science Foundation [19-28323X]
- Biotechnology and Biological Sciences Research Council [BB/R015694/1, BB/E009743/1] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [EP/H024697/1] Funding Source: researchfish
- BBSRC [BB/R015694/1, BB/E009743/1] Funding Source: UKRI
- EPSRC [EP/H024697/1] Funding Source: UKRI
Chlorophyll triplet excited states are byproducts of photosynthetic processes that can indirectly harm biological membranes by forming highly reactive oxygen species. A crucial photoprotective mechanism evolved by plants to counter this threat involves the triplet energy transfer from chlorophylls to carotenoid molecules, in which triplet states are not reactive. In the major light-harvesting complex of photosystem II (LHCII), the two central luteins play an important role in the mechanism, but it has been shown that carotenoid triplets are formed even when other carotenoids replace them in their binding sites. In this work, we have investigated carotenoid triplet formation in LHCII isolated from Arabidopsis thaliana npq1lut2 plants, in which violaxanthin replaces lutein. Although transient absorption spectroscopy showed altered singlet excited-state dynamics in the mutant LHCII without lutein, these antennae formed carotenoid triplets that were spectrally and dynamically identical to the wild-type protein. We conclude that lutein-binding sites in LHCII have conserved characteristics to ensure efficient triplet energy transfer to the carotenoid molecules that they accommodate, making the identity of the carotenoid trivial per se.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据