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Resonance Raman-spectroscopic evidence for the identity of the bacteriochlorophyll-c organization in protein-free and protein-containing chlorosomes from chloroflexus-aurantiacus
Citation key ISI:A1991FJ89800012
Author Hildebrandt, P and Griebenow, K and Holzwarth, A R and Schaffner, K
Pages 228-232
Year 1991
ISSN 0939-5075
Address POSTFACH 2645, W-7400 TUBINGEN, GERMANY
Journal Journal Of Biosciences
Volume 46
Number 3-4
Month MAR-APR
Publisher VERLAG Z NATURFORSCH
Abstract Protein-free and protein-containing chlorosomes from Chloroflexus aurantiacus, strain Ok-70 fl, were studied by resonance Raman (RR) spectroscopy. Both preparations gave the same spectra of the bacteriochlorophyll c (BChl c) chromophores in the range of 1200-1750 cm-1. This strongly corroborates previous evidence [Griebenow et al., Z. Naturforsch. 45 c, 823-828 (1990), and references therein] that the three-dimensional structure of the antenna complexes is not determined by direct interaction with protein but rather is due to BChl c self-organization. The analysis of the coordination-sensitive marker bands of the chlorin macrocycle reveals a mixed six- and fivefold ligation of the Mg ion. Based on two C = O stretching vibrations originating from a free and a Mg-bound C-9 keto group, it is concluded that only in the six-coordinated state the keto group serves as an axial ligand to the Mg ion of a neighbouring chlorin. The second permanently bound axial ligand is attributed to the C-2a hydroxyl group.
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