The long-range supraorganization of the bacterial photosynthetic unit: A key role for PufX
Author(s) -
Raoul N. Frese,
John D. Olsen,
Rikard Branvall,
Willem H.J. Westerhuis,
C. Neil Hunter,
Rienk van Grondelle
Publication year - 2000
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.090083797
Subject(s) - photosynthetic reaction centre , rhodobacter sphaeroides , photosynthesis , purple bacteria , biophysics , electron transfer , membrane , light harvesting complex , chemistry , electrochemical gradient , bacteriochlorophyll , photosystem ii , biology , photochemistry , biochemistry
Bacterial photosynthesis relies on the interplay between light harvesting and electron transfer complexes, all of which are located within the intracytoplasmic membrane. These complexes capture and transfer solar energy, which is used to generate a proton gradient. In this study, we identify one of the factors that determines the organization of these complexes. We undertook a comparison of the organization of the light-harvesting complex 1 (LH1)/reaction center (RC) cores in the LH2(-) mutant of Rhodobacter sphaeroides in the presence or absence of the PufX protein. From polarized absorption spectra on oriented membranes, we conclude that PufX induces a specific orientation of the reaction center in the LH1 ring, as well as the formation of a long-range regular array of LH1-RC cores in the photosynthetic membrane. From our data, we have constructed a precise model of how the RC is positioned within the LH1 ring relative to the long (orientation) axis of the photosynthetic membrane.
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