Mechanisms of Lipid-protein Binding in Photosynthetic Membranes
The lipids of photosynthetic membranes can be divided into two groups on the basis of their protein-binding properties. Most of the non-acyl lipids, such as the chlorophylls, carotenoids and xanthophylls, are relatively tightly, albeit non-covalently, bound to protein ligands. On the other hand, the acyl lipids are not tightly bound to membrane proteins, although there may be specific interactions between them. Some lipids, such as the quinones fall into both categories. There are specific quinone-binding sites on several thylakoid proteins at which quinones or their derivitives are tightly bound, e.g., some proteins of the cytochrome b6-f and the QA site of PSII (1). There are, however, other quinone-binding sites where the quinones are free to exchange with a mobile quinone population in the acyl lipid bilayer, e.g. the QB site of the 32kDa herbicide-binding protein of PSII (1).
KeywordsThylakoid Membrane Lipid Class Photosynthetic Membrane Acyl Lipid Thylakoid Protein
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- 1.Murphy, D.J. (1986) Biochim. Biophys Acta 864, 33–95Google Scholar
- 2.Fish, L.E., Kuk, U., Bogorad, L. (1985) J. Bil. Chem. 260, 1413–1421Google Scholar
- 6.Murphy, D.J. (1986) In: From Structural Elucidation to Biological Function — Current Topics in Lipid Research, Klein, R. and Schmitz, B., eds, Royal Society of Chemistry, London, in pressGoogle Scholar
- 8.Deveaux, P.F. and Seigneuret, M. (1985) Biochim. Biophys. Acta 822, 63–125Google Scholar
- 10.Murphy, D.J. and Knowles, P.F. (1984) In: Structure, Function and Metabolism of Plant Lipids, pp 425–428, Siegenthaler, P.A. and Eichenberger, E., eds, Elsevier, Amsterdam.Google Scholar