Abstract:
:Stark absorption spectroscopy was applied to clarify the structural differences between carotenoids bound to the B800-820 and B800-850 LH2 complexes from a purple photosynthetic bacterium Phaeospirillum (Phs.) molischianum DSM120. The former complex is produced when the bacteria are grown under stressed conditions of low temperature and dim light. These two LH2 complexes bind carotenoids with similar composition, 10% lycopene and 80% rhodopin, each with the same number of conjugated CC double bonds (n=11). Quantitative classical and semi-quantum chemical analyses of Stark absorption spectra recorded in the carotenoid absorption region reveal that the absolute values of the difference dipole moments |Δμ| have substantial differences (2 [D/f]) for carotenoids bound to either B800-820 or B800-850 complexes. The origin of this striking difference in the |Δμ| values was analyzed using the X-ray crystal structure of the B800-850 LH2 complex from Phs. molischianum DSM119. Semi-empirical molecular orbital calculations predict structural deformations of the major carotenoid, rhodopin, bound within the B800-820 complex. We propose that simultaneous rotations around neighboring CC and CC bonds account for the differences in the 2 [D/f] of the |Δμ| value. The plausible position of the rotation is postulated to be located around C21-C24 bonds of rhodopin.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Horibe T,Qian P,Hunter CN,Hashimoto Hdoi
10.1016/j.abb.2014.12.015subject
Has Abstractpub_date
2015-04-15 00:00:00pages
158-166eissn
0003-9861issn
1096-0384pii
S0003-9861(14)00431-7journal_volume
572pub_type
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更新日期:2011-10-01 00:00:00
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journal_title:Archives of biochemistry and biophysics
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