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Papers In Press, published online ahead of print September 22, 2003
Dipartimento Scientifico e Tecnologico, Università di Verona, Verona 37134
Corresponding Author: bassi{at}sci.univr.it
Photosystem I of higher plants is characterised by a typical long wavelength fluorescence emission associated to its LHCI moiety. The origin of these low energy chlorophyll spectral forms was investigated by using site-directed mutagenesis of Lhca1-4 genes and in vitro reconstitution into recombinant pigment-protein complexes. We showed that the red-shifted absorption originates from Chl-Chl excitonic interactions involving Chl A5 in each of the four Lhca antenna complexes. An essential requirement for the presence of the red-shifted absorption/fluorescence spectral forms was the presence of asparagine as ligand for the Chl a chromophore in the binding site A5 of Lhca complexes. In Lhca3 and Lhca4, which exhibit the most red-shifted red forms, its substitution by histidine maintains the pigment binding and yet the red spectral forms are abolished. Conversely, in Lhca1, having very low amplitude of red forms, the substitution of Asn for His produces a red shift of the fluorescence emission thus confirming that the nature of the Chl A5 ligand determines the correct organisation of chromophores leading to excitonic interaction responsible for the red-most forms. The red-shifted fluorescence emission at 730 nm is here proposed to originate from an absorption band around 700 nm, which represents the low-energy contribution of an excitonic interaction having the high-energy band at 683 nm. Since the mutation does not affect Chl A5 orientation, we suggest that coordination by Asn of Chl A5 holds it at the correct distance with Chl B5.
J. Biol. Chem, 10.1074/jbc.M309203200
Submitted on August 19, 2003
Revised on September 21, 2003
Accepted on September 22, 2003
The nature of a chlorophyll ligand in Lhca proteins determines the far red fluorescence emission typical of photosystem I
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