Characterization of the Different Peripheral Light-Harvesting Complexes from High- and Low-Light Grown Cells fromRhodopseudomonas palustris†

Biochemistry ◽  
1999 ◽  
Vol 38 (16) ◽  
pp. 5185-5190 ◽  
Author(s):  
Andrew Gall ◽  
Bruno Robert
Keyword(s):  
Light Harvesting ◽  
Low Light ◽  
Light Harvesting Complexes

scholarly journals Low Light Adaptation: Energy Transfer Processes in Different Types of Light Harvesting Complexes from Rhodopseudomonas palustris

2009 ◽  
Vol 97 (11) ◽  
pp. 3019-3028 ◽  
Author(s):  
Vladimíra Moulisová ◽  
Larry Luer ◽  
Sajjad Hoseinkhani ◽  
Tatas H.P. Brotosudarmo ◽  
Aaron M. Collins ◽  
...  
Keyword(s):  
Energy Transfer ◽  
Light Adaptation ◽  
Light Harvesting ◽  
Rhodopseudomonas Palustris ◽  
Low Light ◽  
Light Harvesting Complexes ◽  
Transfer Processes ◽  
Different Types

scholarly journals The light intensity under which cells are grown controls the type of peripheral light-harvesting complexes that are assembled in a purple photosynthetic bacterium

2011 ◽  
Vol 440 (1) ◽  
pp. 51-61 ◽  
Author(s):  
Tatas H. P. Brotosudarmo ◽  
Aaron M. Collins ◽  
Andrew Gall ◽  
Aleksander W. Roszak ◽  
Alastair T. Gardiner ◽  
...  
Keyword(s):  
Light Intensity ◽  
Light Harvesting ◽  
Rhodopseudomonas Palustris ◽  
Photosynthetic Bacterium ◽  
Low Light ◽  
Light Harvesting Complexes ◽  
Density Maps ◽  
Purple Photosynthetic Bacterium ◽  
Resonance Raman Spectra ◽  
Apoprotein Composition

The differing composition of LH2 (peripheral light-harvesting) complexes present in Rhodopseudomonas palustris 2.1.6 have been investigated when cells are grown under progressively decreasing light intensity. Detailed analysis of their absorption spectra reveals that there must be more than two types of LH2 complexes present. Purified HL (high-light) and LL (low-light) LH2 complexes have mixed apoprotein compositions. The HL complexes contain PucABa and PucABb apoproteins. The LL complexes contain PucABa, PucABd and PucBb-only apoproteins. This mixed apoprotein composition can explain their resonance Raman spectra. Crystallographic studies and molecular sieve chromatography suggest that both the HL and the LL complexes are nonameric. Furthermore, the electron-density maps do not support the existence of an additional Bchl (bacteriochlorophyll) molecule; rather the density is attributed to the N-termini of the α-polypeptide.

scholarly journals Non-conventional octameric structure of C-phycocyanin

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Takuo Minato ◽  
Takamasa Teramoto ◽  
Naruhiko Adachi ◽  
Nguyen Khac Hung ◽  
Kaho Yamada ◽  
...  
Keyword(s):  
Analytical Ultracentrifugation ◽  
Light Harvesting ◽  
Blue Pigment ◽  
Intermediate Structure ◽  
Transfer Energy ◽  
Light Harvesting Complexes ◽  
Photosystems I And Ii ◽  
Light Harvesting Antenna ◽  
First Time

AbstractC-phycocyanin (CPC), a blue pigment protein, is an indispensable component of giant phycobilisomes, which are light-harvesting antenna complexes in cyanobacteria that transfer energy efficiently to photosystems I and II. X-ray crystallographic and electron microscopy (EM) analyses have revealed the structure of CPC to be a closed toroidal hexamer by assembling two trimers. In this study, the structural characterization of non-conventional octameric CPC is reported for the first time. Analyses of the crystal and cryogenic EM structures of the native CPC from filamentous thermophilic cyanobacterium Thermoleptolyngbya sp. O–77 unexpectedly illustrated the coexistence of conventional hexamer and novel octamer. In addition, an unusual dimeric state, observed via analytical ultracentrifugation, was postulated to be a key intermediate structure in the assemble of the previously unobserved octamer. These observations provide new insights into the assembly processes of CPCs and the mechanism of energy transfer in the light-harvesting complexes.

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