The core complex formed by the reaction center and the light harvesting complex 1 (RC-LH1) was purified from the photosynthetic bacterium Rhodobacter sphaeroides. We analyzed the lipid and ubiquinone (UQ) complements copurifying with the RC-LH1 complex and with the peripheral antenna (LH2). ln RC-LH1 UQ was almost ten times more concentrated than in the LH2 and in the native membranes from which the complexes were extracted. The fractional lipid composition of the RC-LH1 complex also differed from that of lhe intact membranes, exhibiting a marked increase in cardiolipin concentration. We propose that the confinement of cardiolipin and ubiquinone observed within the RC-LH1 complex, plays a role in vivo in lhe stabilization of the light-induced charge separation catalyzed by the RC.

Confinement of cardiolipin and ubiquinone in reaction center core complexes purified from the photosynthetic bacterium Rhodobacter sphaeroides

DEZI, MANUELA;FRANCIA, FRANCESCO;VENTUROLI, GIOVANNI
2007

Abstract

The core complex formed by the reaction center and the light harvesting complex 1 (RC-LH1) was purified from the photosynthetic bacterium Rhodobacter sphaeroides. We analyzed the lipid and ubiquinone (UQ) complements copurifying with the RC-LH1 complex and with the peripheral antenna (LH2). ln RC-LH1 UQ was almost ten times more concentrated than in the LH2 and in the native membranes from which the complexes were extracted. The fractional lipid composition of the RC-LH1 complex also differed from that of lhe intact membranes, exhibiting a marked increase in cardiolipin concentration. We propose that the confinement of cardiolipin and ubiquinone observed within the RC-LH1 complex, plays a role in vivo in lhe stabilization of the light-induced charge separation catalyzed by the RC.
Dezi M.; Francia F.; Mallardi A.; Palazzo G.; Venturoli G
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11585/130667
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