Abstract
The structure of the light-harvesting (LH) complexes of the purple photosynthetic bacteria are unique in that small polypeptides (5 to 10 kd) are responsible for binding bacteriochlorophyll (BChl) and carotenoid (Car) pigments in a very specific relationship to each other, to the membrane, and to the reaction center (RC). These polypeptides are so small that they only span the membrane once, and a high percentage (approximately 25%) of the total mass of the LH complexes are due to BChl and Car. Thus, before they were ever isolated, it was clear that these LH complexes must carry out much of their function through interaction with associated subunits. Our goal has been to isolate the core BChl LH complex (B873) from Rhodospirillum rubrum and reversibly dissociate it into its subunit forms so that we could systematically study its structure-function relationships by selective group modification. A further goal is to dissociate the complex into free polypeptides and BChl and then reassociate these to form the in vivo complex.
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References
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© 1987 Martinus Nijhoff Publishers, Dordrecht
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Parkes-Loach, P., Riccobono, J., Loach, P. (1987). Preparation of Subunit Forms of the Light-Harvesting Complex of Rhodospirillum Rubrum . In: Biggins, J. (eds) Progress in Photosynthesis Research. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-3535-8_6
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DOI: https://doi.org/10.1007/978-94-009-3535-8_6
Publisher Name: Springer, Dordrecht
Print ISBN: 978-94-010-8080-4
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