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Oligomerization state and pigment binding strength of the peridinin‐Chl a ‐protein
Author(s) -
Jiang Jing,
Zhang Hao,
Lu Xun,
Lu Yue,
Cuneo Matthew J.,
O'Neill Hugh M.,
Urban Volker,
Lo Cynthia S.,
Blankenship Robert E.
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.07.039
Subject(s) - peridinin , dinoflagellate , monomer , symbiodinium , chemistry , size exclusion chromatography , pigment , photosynthesis , chlorophyll a , light harvesting complex , biophysics , biochemistry , photochemistry , carotenoid , biology , botany , fucoxanthin , photosystem ii , organic chemistry , genetics , symbiosis , bacteria , enzyme , polymer
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.