Core mutations of Synechococcus sp. PCC 7002 phycobilisomes

A spectroscopic study

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

Research output: Contribution to journalArticleResearchpeer-review

32 Citations (Scopus)

Abstract

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 L99 CM 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
Volume15
Issue number1-2
DOIs
StatePublished - 14 Aug 1992

Fingerprint

Phycobilisomes
Synechococcus
mutations
fluorescence
Mutation
chromophores
Fluorescence
antiphase boundaries
cysteine
polypeptides
kinetics
emission spectra
absorption spectra
Serine
Cysteine
Peptides

Keywords

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

Cite this

Gindt, Yvonne ; Zhou, Jianhui ; Bryant, Donald A. ; Sauer, Kenneth. / Core mutations of Synechococcus sp. PCC 7002 phycobilisomes : A spectroscopic study. In: Journal of Photochemistry and Photobiology, B: Biology. 1992 ; Vol. 15, No. 1-2. pp. 75-89.
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abstract = "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 L99 CM 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.",
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Core mutations of Synechococcus sp. PCC 7002 phycobilisomes : A spectroscopic study. / Gindt, Yvonne; Zhou, Jianhui; Bryant, Donald A.; Sauer, Kenneth.

In: Journal of Photochemistry and Photobiology, B: Biology, Vol. 15, No. 1-2, 14.08.1992, p. 75-89.

Research output: Contribution to journalArticleResearchpeer-review

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