Functional assignment of chromophores and energy transfer in C phycocyanin isolated from the thermophilic cyanobacterium Mastigocladus laminosus |
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| Affiliation: | 1. Institute of Pharmaceutical Technology and Biopharmacy, University of Münster, Corrensstraße 48, 48149 Münster, Germany;2. Institute of Pharmaceutical Science, King’s College London, Franklin-Wilkins Building, 150 Stamford Street, London, SE1 9NH, UK;1. Kazakh National Research Technical University Named After K.I. Satpayev, Almaty, Kazakhstan;2. Max-Planck Institute of Colloids and Interfaces, Potsdam, Golm, Germany;3. Universidade Nova de Lisboa, Lisboa, Portugal;1. Department of Food Science and Technology, Federal University of Santa Maria (UFSM), 97105-900 Santa Maria, RS, Brazil;2. Food Phytochemistry Department, Instituto de la Grasa (CSIC), University Campus, Building 46, 41013 Sevilla, Spain;1. Institute of Biological and Medical Imaging (IBMI), Helmholtz Zentrum München, Neuherberg, Germany;2. Intracellular Transport and RNA Biology Group, Institute of Structural Biology, Helmholtz Zentrum München, Neuherberg, Germany;4. Institute of Pharmaceutical Biotechnology, Ulm University, Ulm, Germany;5. Chair of Biological Imaging, Technische Universität München, Munich, Germany;6. Center for Translational Cancer Research (TranslaTUM), Technische Universität München, Munich, Germany;1. Department of Organic Chemistry, Arrhenius Laboratory, Stockholm University, S-106 91 Stockholm, Sweden;2. Institute of Agro-Food Technology, Jilin Academy of Agricultural Sciences, Changchun 130033, PR China;3. School of Food Science, Beijing Technology and Business University, Beijing 100048, PR China |
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| Abstract: | The optical characteristics and pathway of energy transfer in the C phycocyanin trimer isolated from the thermophilic cyanobacterium Mastigocladus laminosus were investigated at steady state by absorption, circular dichroism, fluorescence and fluorescence polarization spectroscopy. Based on the comparison of optical data with the 3-dimensional structure of the C-phycocyanin trimer determined by X-ray analysis (Schirmer, T., Bode, W., Huber, R., Sidler, W. and Zuber, H. (1984) in Proceedings of the Symposium on Optical Properties and Structure of Tetrapyrroles, (Blauer, G. and Sund, M., eds.), pp. 445–449, Walter de Gruyter, Berlin, and (1985) J. Mol. Biol. 184, 257–277), the functional assignment of three types of chromophore was established. An α subunit has an s chromophore and the chromophores at the positions 84 and 155 in the amino acid sequence of the β subunit are assigned as f and s chromophores, respectively. In the C phycocyanin trimer energy transfer occurs from the α chromophore in one monomer to the βf chromophore in an adjacent monomer, and from the βs chromophore to the βf chromophore in the same monomer. The direction of energy flow is from the outside to the inside of the trimer, where the locus for the binding of a colourless polypeptide is postulated. In the phycobilisomes the energy concentrated at the βf chromophores might be transferred toward the allophycocyanin core mainly by the βf chromophores in the phycocyanin rods. |
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