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Structure of a photosystem II supercomplex isolated from Prochlorion didemni retaining its chlorophyll a/b light-harvesting system
被引:62
作者:
Bibby, TS
Nield, J
Chen, M
Larkum, AWD
Barber, J
[1
]
机构:
[1] Univ London Imperial Coll Sci Technol & Med, Wolfson Labs, Dept Sci Biol, London SW7 2AZ, England
[2] Univ Sydney, Sydney, NSW 2006, Australia
来源:
关键词:
D O I:
10.1073/pnas.1532271100
中图分类号:
O [数理科学和化学];
P [天文学、地球科学];
Q [生物科学];
N [自然科学总论];
学科分类号:
07 ;
0710 ;
09 ;
摘要:
Prochlorophytes are a class of cyanobacteria that do not use phycobiliproteins as light-harvesting systems, but contain chlorophyll (Chl) a/b-binding Pcb proteins. Recently it was shown that Pcb proteins form an 18-subunit light-harvesting antenna ring around the photosystem I (PSI) trimeric reaction center complex of the prochlorophyte Prochlorococcus marinus SS120. Here we have investigated whether the symbiotic prochlorophyte Prochloron didemni also contains the same supermolecular complex. Using cells isolated directly from its ascidian host, we found no evidence for the presence of the Pcb-PSI supercomplex. Instead we have identified and characterized a supercomplex composed of photosystem II (PSII) and Pcb proteins. We show that 10-Pcb subunits associate with the PSII dimeric reaction center core to form a giant complex having an estimated M-r of 1,500 kDa with dimensions of 210 x 290 Angstrom. Five-Pcb subunits flank each long side of the dimer and assuming each binds 13 Chl molecules, increase the antenna size of PSR by approximate to200%. Fluorescence emission studies indicate that energy transfer occurs efficiently from the Pcb antenna. Modeling using the x-ray structure of cyanobacterial PSII suggests that energy transfer to the PSII reaction center is via the Chls bound to the CP47 and CP43 proteins.
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页码:9050 / 9054
页数:5
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