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.

doi:10.1016/j.febslet.2015.07.039

Oligomerization state and pigment binding strength of the peridinin-Chl a -protein

Journal Article · Sat Aug 01 04:00:00 EDT 2015 · FEBS Letters

DOI:https://doi.org/10.1016/j.febslet.2015.07.039· OSTI ID:1352750

Jiang, Jing ^[1]; Zhang, Hao ^[2]; Lu, Xun ^[3]; Lu, Yue ^[2]; Cuneo, Matthew J. ^[3]; O'Neill, Hugh M. ^[3]; Urban, Volker ^[3]; Lo, Cynthia S. ^[1]; Blankenship, Robert E. ^[4]

Washington University in St. Louis, MO (United States). Department of Energy, Environmental & Chemical Engineering
Washington University in St. Louis, MO (United States). Department of Chemistry
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States). Center for Structural Molecular Biology, Biology and Soft Matter Division
Washington University in St. Louis, MO (United States). Department of Chemistry and Department of Biology

The peridinin-chlorophylla-protein (PCP) is one of the major light harvesting complexes (LHCs) in photosynthetic dinoflagellates. For this research, we analyzed the oligomeric state of PCP isolated from the dinoflagellateSymbiodinium, 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. Lastly, the trimerization may not be necessary for PCP to function as a light-harvesting complex.

Research Organization:: Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)

DOE Contract Number:: AC05-00OR22725; SC0001035

OSTI ID:: 1352750

Journal Information:: FEBS Letters, Journal Name: FEBS Letters Journal Issue: 19PartB Vol. 589; ISSN 0014-5793

Publisher:: Federation of European Biochemical Societies

Country of Publication:: United States

Language:: English

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Oligomerization state and pigment binding strength of the peridinin-Chl a -protein

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