Core mutations of Synechococcus sp. PCC 7002 phycobilisomes: A spectroscopic study

Yvonne M. Gindt, Jianhui Zhou, Donald A. Bryant, Kenneth Sauer

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Three cyanobacterial strains harboring mutations affecting phycobilisome (PBS) cores were studied using steady state absorption and fluorescence and time-resolved fluorescence. The apcF mutant, missing β18, and the apcDF mutant, missing both αAPB and β18P, showed only small spectroscopic differences from the wild-type strain; their PBS emission was blue shifted by 10 nm, whereas their absorption spectra and time-resolved fluorescence kinetics were virtually unchanged. The third mutant studied was the apcE/C186S mutant in which the chromophore-binding cysteine-186 in the L99CM polypeptide has been substituted with serine. The apcE/C186S mutant contained a modified chromophore which significantly changed the spectroscopic properties of the PBS complex. The apcE/C186S PBS absorbed more than the wild-type strain at 705 nm, and the emission spectrum gave two peaks at 660 nm and 715 nm. The time-resolved kinetics of the apcE/C186S mutant PBS were also significantly altered from those of the wild-type strain.

Original languageEnglish
Pages (from-to)75-89
Number of pages15
JournalJournal of Photochemistry and Photobiology, B: Biology
Issue number1-2
StatePublished - 14 Aug 1992


  • Phycobilisome
  • apcDF mutant
  • apcE/C186S mutant.
  • apcf mutant
  • cyanobacteria
  • fluorescence relaxation


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