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A stable ‘sandwich’ system of Surface-Enhanced Resonance Raman Scattering for the analysis of β-carotenes in a photosynthetic pigment-protein complex

Authors


  • Xiaochun Qin and Jiajia Zhu contributed equally to this work.

Correspondence to: Yan Fang, Beijing Key Laboratory for Nano-Photonics and Nano-Structure, Capital Normal University, Beijing 100048, China

E-mail: wedu@263.net

Correspondence to: Tingyun Kuang, Photosynthesis Research Center, Key Laboratory of Photobiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China

E-mail: kuangty@ibcas.ac.cn

Abstract

In plants, Photosystem I (PSI) is composed of a core complex and a membrane-associated antenna complex light-harvesting complex I that captures light and funnels its energy to the core complex. To obtain Raman structural information on β-carotenes embedded in the PSI core complex, a ‘sandwich’ system of roughened silver slice: target protein complexes: single silver nanoparticles was fabricated for Surface-Enhanced Resonance Raman Scattering (SERRS) measurements. This study provided a method to overcome spectral irreproducibility, which is the main drawback of Surface-Enhanced Raman Scattering/SERRS-based studies. The Raman spectra of β-carotenes embedded in the PSI core complex can be obtained at very low sample concentrations (1–5 µg Chl/ml) and high signal/noise ratios. The β-carotenes in the spinach PSI core complex were predominantly all-trans configuration. The membrane protein-mediated adsorption of silver nanoparticles induced the uniform distribution of a large number of single nanoparticles, which contributed to achieving highly reproducible SERRS spectra. This study is the first to apply single silver nanoparticle-based SERRS analysis in membrane proteins. Copyright © 2013 John Wiley & Sons, Ltd.

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