4.4 Article Proceedings Paper

Picosecond excitation energy transfer of allophycocyanin studied in solution and in crystals

期刊

PHOTOSYNTHESIS RESEARCH
卷 135, 期 1-3, 页码 79-86

出版社

SPRINGER
DOI: 10.1007/s11120-017-0417-4

关键词

Allophycocyanin crystals; Excitation energy transfer; Phycobilisome; Cyanobacteria; Time-resolved fluorescence spectroscopy

资金

  1. Foundation for Fundamental Research on Matter (FOM), which is part of The Netherlands Organization for Scientific Research (NWO) [10TBSC24-3]
  2. Dutch Ministry of Economic Affairs
  3. University Grants Commissions (UGC), New Delhi

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Cyanobacteria perform photosynthesis with the use of large light-harvesting antennae called phycobilisomes (PBSs). These hemispherical PBSs contain hundreds of open-chain tetrapyrrole chromophores bound to different peptides, providing an arrangement in which excitation energy is funnelled towards the PBS core from where it can be transferred to photosystem I and/or photosystem II. In the PBS core, many allophycocyanin (APC) trimers are present, red-light-absorbing phycobiliproteins that covalently bind phycocyanobilin (PCB) chromophores. APC trimers were amongst the first light-harvesting complexes to be crystallized. APC trimers have two spectrally different PCBs per monomer, a high- and a low-energy pigment. The crystal structure of the APC trimer reveals the close distance (21 ) between those two chromophores (the distance within one monomer is 51 ) and this explains the ultrafast (1 ps) excitation energy transfer (EET) between them. Both chromophores adopt a somewhat different structure, which is held responsible for their spectral difference. Here we used spectrally resolved picosecond fluorescence to study EET in these APC trimers both in crystallized and in solubilized form. We found that not all closely spaced pigment couples consist of a low- and a high-energy pigment. In 10% of the cases, a couple consists of two high-energy pigments. EET to a low-energy pigment, which can spectrally be resolved, occurs on a time scale of tens of picoseconds. This transfer turns out to be three times faster in the crystal than in the solution. The spectral characteristics and the time scale of this transfer component are similar to what have been observed in the whole cells of Synechocystis sp. PCC 6803, for which it was ascribed to EET from C-phycocyanin to APC. The present results thus demonstrate that part of this transfer should probably also be ascribed to EET within APC trimers.

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