Resonance Raman Spectroscopic Evidence for the Identity of the Bacteriochlorophyll c Organization in Protein-Free and Protein-Containing Chlorosomes from Chloroflexus auvantiacus release_wu5mrrldrfedtclohcu4j3rctu

by Peter Hildebrandt, Kai Griebenow, Alfred R. Holzwarth, Kurt Schaffner

Published in Zeitschrift für Naturforschung C - A Journal of Biosciences by Walter de Gruyter GmbH.

1991   Volume 46, Issue 3-4, p228-232

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<jats:sup>-1</jats:sup>. This strongly corroborates previous evidence [Griebenow et al., Z. Naturforsch. 45c, 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 selforganization. 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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