Increasing the absorption
cross section of plants by introducing
far-red absorbing chlorophylls (Chls) has been proposed as a strategy
to boost crop yields. To make this strategy effective, these Chls
should bind to the photosynthetic complexes without altering their
functional architecture. To investigate if plant-specific antenna
complexes can provide the protein scaffold to accommodate these Chls,
we have reconstituted the main light-harvesting complex (LHC) of plants
LHCII
in vitro
and
in silico
, with
Chl
d
. The results demonstrate that LHCII can bind
Chl
d
in a number of binding sites, shifting the
maximum absorption ∼25 nm toward the red with respect to the
wild-type complex (LHCII with Chl
a
and
b
) while maintaining the native LHC architecture. Ultrafast spectroscopic
measurements show that the complex is functional in light harvesting
and excitation energy transfer. Overall, we here demonstrate that
it is possible to obtain plant LHCs with enhanced far-red absorption
and intact functional properties.
Carotenoids are essential constituents of plant light-harvesting complexes (LHCs), being involved in protein stability, light harvesting, and photoprotection. Unlike chlorophylls, whose binding to LHCs is known to require coordination of...
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