Comparison of calculated and experimentally resolved rate constants for excitation energy transfer in C-phycocyanin. 1. Monomers
- Lawrence Berkeley Lab., CA (United States)
- Pennsylvania State Univ., University Park, PA (United States)
Rate constants for excitation energy transfer in light-harvesting protein, C-phycocyanin (PC), in the monomeric aggregation state, isolated from the cyanobacterium cynechococcus sp. PCC 7002, are calculated, using Foerster theory and compared with the results of time-resolved fluorescence measurements. The assignments of the energy-transfer rate constants in PC monomers are confirmed here by time-resolved fluorescence anisotropy measurements of the PC monomers isolated from both the wild-type and a mutant strain (cpcB/C155S) whose PC is missing the {beta}{sub 155} chromophore. It is concluded that the Foerster model of resonant energy transfer in the weak coupling limit successfully describes the dominant energy-transfer processes in this protein in the monomeric state. 31 refs., 3 figs., 4 tabs.
- Sponsoring Organization:
- USDOE
- DOE Contract Number:
- AC03-76SF00098
- OSTI ID:
- 62306
- Journal Information:
- Journal of Physical Chemistry, Vol. 99, Issue 20; Other Information: PBD: 18 May 1995
- Country of Publication:
- United States
- Language:
- English
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