title: Oligomerization state and pigment binding strength of the peridinin-Chl a-protein.
abstract: The 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.
authors.affiliation: Department of Energy, Environmental & Chemical Engineering, Washington University in St. Louis, St. Louis, MO 63130, USA.
authors.forename: Jing
authors.initials: J
authors.lastname: Jiang
authors.affiliation: Department of Chemistry, Washington University in St. Louis, St. Louis, MO 63130, USA.
authors.forename: Hao
authors.initials: H
authors.lastname: Zhang
authors.affiliation: Center for Structural Molecular Biology, Biology and Soft Matter Division, Oak Ridge National Laboratory, Oak Ridge, TN 37831, USA.
authors.forename: Xun
authors.initials: X
authors.lastname: Lu
authors.affiliation: Department of Chemistry, Washington University in St. Louis, St. Louis, MO 63130, USA.
authors.forename: Yue
authors.initials: Y
authors.lastname: Lu
authors.affiliation: Center for Structural Molecular Biology, Biology and Soft Matter Division, Oak Ridge National Laboratory, Oak Ridge, TN 37831, USA.
authors.forename: Matthew J
authors.initials: MJ
authors.lastname: Cuneo
authors.affiliation: Center for Structural Molecular Biology, Biology and Soft Matter Division, Oak Ridge National Laboratory, Oak Ridge, TN 37831, USA.
authors.forename: Hugh M
authors.initials: HM
authors.lastname: O'Neill
authors.affiliation: Center for Structural Molecular Biology, Biology and Soft Matter Division, Oak Ridge National Laboratory, Oak Ridge, TN 37831, USA.
authors.forename: Volker
authors.initials: V
authors.lastname: Urban
authors.affiliation: Department of Energy, Environmental & Chemical Engineering, Washington University in St. Louis, St. Louis, MO 63130, USA.
authors.forename: Cynthia S
authors.initials: CS
authors.lastname: Lo
authors.affiliation: Department of Chemistry, Washington University in St. Louis, St. Louis, MO 63130, USA; Department of Biology, Washington University in St. Louis, St. Louis, MO 63130, USA. Electronic address: blankenship@wustl.edu.
authors.forename: Robert E
authors.initials: RE
authors.lastname: Blankenship
mesh_terms: D004141:Dinoflagellida / Q000201:enzymology; D045342:Light-Harvesting Protein Complexes / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D010860:Pigments, Biological / Q000378:metabolism*; D011485:Protein Binding; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary
chemical_list: D045342:Light-Harvesting Protein Complexes; D010860:Pigments, Biological
keywords: Chlorophyll; Dinoflagellate; Light-harvesting; Native mass spectrometry; Peridinin; Photosynthesis; Symbiodinium