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Originally published In Press as doi:10.1074/jbc.M000658200 on May 9, 2000

J. Biol. Chem., Vol. 275, Issue 29, 22031-22036, July 21, 2000
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Pigment Binding Site Properties of Two Photosystem II Antenna Proteins
A RESONANCE RAMAN INVESTIGATION*

Andy PascalDagger §, Ulrich Wacker||**, Klaus-Dieter Irrgang**, Peter Horton||, Gernot Renger, and Bruno RobertDagger

From the Dagger  Section de Biophysique des Protéines et des Membranes, Département de Biologie Cellulaire et Moléculaire, Commissariat à l'Energie Atomique and URA 2096, Centre National de la Recherche Scientifique, CE-Saclay, F-91191 Gif-sur-Yvette, France, the  Max-Völmer Institut für Biophysikalische Chemie und Biochemie, Technische Universität Berlin, Straße des 17, Juni 135, D-10623 Berlin, PC 14, Germany, and the || Robert Hill Institute, Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield S10 2UH, United Kingdom

Two light-harvesting proteins associated with photosystem II of higher plants, namely the major antenna complex LHCIIb and the minor Lhcb4 protein (CP29), have been investigated by resonance Raman spectroscopy. One of the two chlorophylls b and up to five of the six chlorophylls a present in Lhcb4 are shown to adopt similar binding conformations to the (presumably) corresponding molecules in LHCIIb, whereas at least two chlorophylls in the former protein assume unique conformations relative to the bulk complex. The overall conformation of bound xanthophyll molecules is identical in the two antenna proteins, although some small differences are apparent. The pigment binding properties of these two LHCs are discussed, with particular reference to possible structural motifs within this extended family of proteins.

* This work was in part funded by a European Union Human Capital and Mobility grant.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Supported by a Federation of European Biochemical Societies postdoctoral fellowship. To whom correspondence should be addressed: Università di Verona, Facoltà di Scienze MM.FF.NN., Biotechnologie Vegetali, Strada Le Grazie, 37134 Verona, Italy. Tel.: 39-045-809-8915; Fax: 39-045-809-8929; E-mail: andypascal@yahoo.com.

** Funded by Deutsche Forschungsgemeinschaft Grant SFB 312.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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