Investigation of detergent effects on the solution structure of spinach Light Harvesting Complex II

Abstract

The properties of spinach light harvesting complex II (LHC II), stabilized in the detergents Triton X-100 (TX100) and n-Octyl-β-D-Glucoside (BOG), were investigated by small-angle neutron scattering (SANS). The LHC II-BOG scattering curve overlaid well with the theoretical scattering curve generated from the crystal structure of LHC II indicating that the protein preparation was in its native functional state. On the other hand, the simulated LHC II curve deviated significantly from the LHC II-TX100 experimental data. Analysis by circular dichroism spectroscopy supported the SANS analysis and showed that LHC II-TX100 is inactivated. This investigation has implications for extracting and stabilizing photosynthetic membrane proteins for the development of biohybrid photoconversion devices. © 2010 IOP Publishing Ltd.