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Biophysical Journal 86:2363-2373 (2004)
© 2004 The Biophysical Society

In Vitro Self-Assembly of the Light Harvesting Pigment-Protein LH2 Revealed by Ultrafast Spectroscopy and Electron Microscopy

Axel Schubert *, Anna Stenstam {dagger}, Wichard J. D. Beenken *, Jennifer L. Herek {ddagger}, Richard Cogdell §, Tõnu Pullerits * and Villy Sundström *

* Chemical Physics, {dagger} Physical Chemistry 1, Lund University, Lund, Sweden; {ddagger} Fundamenteel Onderzoek der Materie, Institute for Atomic and Molecular Physics, Amsterdam, The Netherlands; and § Biochemistry and Molecular Biology, Glasgow University, Glasgow, United Kingdom

Correspondence: Address reprint requests to Villy Sundstrom, E-mail: villy.sundstrom{at}chemphys.lu.se.

Controlled ensemble formation of protein-surfactant systems provides a fundamental concept for the realization of nanoscale devices with self-organizing capability. In this context, spectroscopic monitoring of pigment-containing proteins yields detailed structural information. Here we have studied the association behavior of the bacterial light-harvesting protein LH2 from Rhodobacter spheroides in an n,n-dimethyldodecylamine-n-oxide/water environment. Time-resolved studies of the excitation annihilation yielded information about aggregate sizes and packing of the protein complexes therein. The results are compared to transmission electron microscopy images of instantaneously frozen samples. Our data indicate the manifestation of different phases, which are discussed with respect to the thermodynamic equilibrium in ternary protein-surfactant-water systems. Accordingly, by varying the concentration the formation of different types of aggregates can be controlled. Conditions for the appearance of isolated LH2 complexes are defined.




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