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Chromophore assignment in phycoerythrocyanin from Mastigocladus laminosus
Authors:Parbel  Axel  Zhao  Kai-Hong  Breton  Jacques  Scheer  Hugo
Institution:(1) Botanisches Institut der Universität, Menzinger Str. 67, D-80638 München, Germany;(2) Academia Sinica, Institute of Photographic Chemistry, 100101 Beijing, China;(3) Department of Biochemistry and Biophysics, Institute of Life Sciences, Wuhan University, Wuhan, Hubei, 430 072, China;(4) SBE/DBCH, CEA Saclay, 91191 Gif sur Yvette, France
Abstract:The component spectra (maxima of absorption, circular and linear dichroism) of individual chromophores have been assigned for phycoerythrocyanin (PEC) trimer, monomer(s), and its subunits (agr-PEC and beta-PEC) by titration with p-chloromercury-benzene-sulfonate (PCMS), linear dichroism and photochemical transformations, as well as by deconvolution using a lsquobilinrsquo line-shape spectrum based on the agr-84 phycoviolobilin-chromophore in the agr-subunit. The level ordering PVB-agr-84 rarr PCB-beta-155 rarr PCB-beta-84 is the same irrespective of aggregation. Two different monomers (agrbeta) were observed. In 4 M urea, the spectra are appropriately weighted sums of the subunit spectra, whereas in the monomer obtained in 1 M KSCN, both beta-chromophores are red-shifted by 4–5 nm. Formation of trimer (agrbeta)_3gives considerable spectral changes: (1) the absorption is narrowed, which has been rationalized by excitonic coupling between neighbouring monomers, (2) the short wavelength part in the CD spectrum is missing and (3) a fourth band (+) at 528 in the LD spectrum appears. A deconvolution of the trimeric aggregation state using only the lsquobilinrsquo line-shape model is not possible.
Keywords:cyanobacteria  energy transfer  Fischerella PCC 7603  photosynthesis  phycobiliprotein  phycoerythrocyanin
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