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J Biol Chem, Vol. 274, Issue 47, 33510-33521, November 19, 1999
From the Università di Verona, Biotecnologie Vegetali, Strada
Le Grazie, 37134, Verona, Italy
The chromophore binding properties of the higher
plant light-harvesting complex II have been studied by site-directed
mutagenesis of pigment-binding residues. Mutant apoproteins were
overexpressed in Escherichia coli and then refolded
in vitro with purified chromophores to yield holoproteins
selectively affected in chlorophyll-binding sites. Biochemical and
spectroscopic characterization showed a specific loss of pigments and
absorption spectral forms for each mutant, thus allowing identification
of the chromophores bound to most of the binding sites. On these bases
a map for the occupancy of individual sites by chlorophyll a and
chlorophyll b is proposed. In some cases a single mutation led to the
loss of more than one chromophore indicating that four chlorophylls and
one xanthophyll could be bound by pigment-pigment interactions.
Differential absorption spectroscopy allowed identification of the
Qy transition energy level for each chlorophyll within the
complex. It is shown that not only site selectivity is largely
conserved between light-harvesting complex II and CP29 but also the
distribution of absorption forms among different protein domains,
suggesting conservation of energy transfer pathways within the protein
and outward to neighbor subunits of the photosystem.
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