Comparison of calculated and experimentally resolved rate constants for excitation energy transfer in C-phycocyanin. 1. Monomers

M. P. Debreczeny, K. Sauer, J. Zhou, D. A. Bryant

Research output: Contribution to journalArticlepeer-review

58 Scopus citations

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 languageEnglish (US)
Pages (from-to)8412-8419
Number of pages8
JournalJournal of physical chemistry
Volume99
Issue number20
DOIs
StatePublished - 1995

All Science Journal Classification (ASJC) codes

  • Engineering(all)
  • Physical and Theoretical Chemistry

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