Journal
BIOCHEMICAL JOURNAL
Volume 440, Issue -, Pages 51-61Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BJ20110575
Keywords
bacteriochlorophyll; light-harvesting complex; puc gene; purple photosynthetic bacterium; Rhodopseudomonas palustris; X-ray crystallography
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Funding
- Photosynthetic Antenna Research Center (PARC)
- Energy Frontier Research Center
- U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences [DE-SC 0001035]
- Engineering and Physical Sciences Research Council
- Agence Nationale de la Recherche (ANR), France [ANR-07-CEXC-009]
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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 PucAB(a) and PucAB(b) apoproteins. The LL complexes contain PucAB(a), PucAB(d) and PucB(b)-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 alpha-polypeptide.
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