Oligomerization state and pigment binding strength of the peridinin-Chl a-protein
- Jiang, Jing
- Zhang, Hao
- Lu, Xun
- Lu, Yue
- Cuneo, Matthew J.
- O’Neill, Hugh M.
- Urban, Volker
- Lo, Cynthia S.
- Blankenship, Robert E.
Publication date
September 2015
DOI Publisher
Federation of European Biochemical Societies. Published by Elsevier B.V.Abstract
AbstractThe peridinin-chlorophyll a-protein (PCP) is one of the major light harvesting complexes (LHCs) in photosynthetic dinoflagellates. We analyzed the oligomeric state of PCP isolated from the dinoflagellate Symbiodinium, which has received increasing attention in recent years because of its role in coral bleaching. Size-exclusion chromatography (SEC) and small angle neutron scattering (SANS) analysis indicated PCP exists as monomers. Native mass spectrometry (native MS) demonstrated two oligomeric states of PCP, with the monomeric PCP being dominant. The trimerization may not be necessary for PCP to function as a light-harvesting complex
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