Abstract
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 β155 chromophore. It is concluded that the Foerster mogel of resonant energy transfer in the weak coupling limit successfully describes the dominant energy-transfer processes in this protein in the monomeric state.
Original language | English (US) |
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Pages (from-to) | 8412-8419 |
Number of pages | 8 |
Journal | Journal of physical chemistry |
Volume | 99 |
Issue number | 20 |
DOIs | |
State | Published - 1995 |
All Science Journal Classification (ASJC) codes
- General Engineering
- Physical and Theoretical Chemistry