Flexibility and size heterogeneity of the LH1 light harvesting complex revealed by atomic force microscopy: functional significance for bacterial photosynthesis.
Previous electron microscopic studies of bacterial RCLH1 complexes demonstrated both circular and elliptical conformations of the LH1 ring, and this implied flexibility has been suggested to allow passage of quinol from the Q(B) site of the RC to the quinone pool prior to reduction of the cytochrome bc(1) complex. We have used atomic force microscopy to demonstrate that these are just two of many conformations for the LH1 ring, which displays large molecule-to-molecule variations, in terms of both shape and size. This atomic force microscope study has used a mutant lacking the reaction center complex, which normally sits within the LH1 ring providing a barrier to substantial changes in shape. This approach has revealed the inherent flexibility and lack of structural coherence of this complex in a reconstituted lipid bilayer at room temperature. Circular, elliptical, and even polygonal ring shapes as well as arcs and open rings have been observed for LH1; in contrast, no such variations in structure were observed for the LH2 complex under the same conditions. The basis for these differences between LH1 and LH2 is suggested to be the H-bonding patterns that stabilize binding of the bacteriochlorophylls to the LH polypeptides. The existence of open rings and arcs provides a direct visualization of the consequences of the relatively weak associations that govern the aggregation of the protomers (alpha(1)beta(1)Bchl(2)) comprising the LH1 complex. The demonstration that the linkage between adjacent protomer units is flexible and can even be uncoupled at room temperature in a detergent-free membrane bilayer provides a rationale for the dynamic separation of individual protomers, and we may now envisage experiments that seek to prove this active opening process.
Bahatyrova
Svetlana
S
Biophysical Techniques Group, Department of Science and Technology, University of Twente, 7500 AE Enschede, The Netherlands.
Frese
Raoul N
RN
van der Werf
Kees O
KO
Otto
Cees
C
Hunter
C Neil
CN
Olsen
John D
JD
D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D006860:Hydrogen Bonding; D045342:Light-Harvesting Protein Complexes / Q000737:chemistry* / Q000378:metabolism; D018625:Microscopy, Atomic Force / Q000379:methods; D008958:Models, Molecular; D011487:Protein Conformation; D012247:Rhodospirillum rubrum / Q000378:metabolism / Q000648:ultrastructure
D001426:Bacterial Proteins; D045342:Light-Harvesting Protein Complexes; C094744:light-harvesting complex 1, Rhodospirillum