Chloroplast protein phosphorylation couples plastoquinone redox state to distribution of excitation energy between photosystems

John F. Allen, John Bennett, Katherine E. Steinback, Charles J. Arntzen

Research output: Contribution to journalArticle

476 Citations (Scopus)

Abstract

In photosynthetic membranes isolated from pea leaves, the redox state of the plastoquinone pool controls both the level of phosphorylation of the chloroplast light-harvesting pigment-protein complex (LHC) and distribution of absorbed excitation energy between the two photosystems. Phosphorylation of LHC polypeptides is proposed as the regulatory mechanism by which photosynthetic systems adapt to changing wavelengths of light.

Original languageEnglish (US)
Pages (from-to)25-29
Number of pages5
JournalNature
Volume291
Issue number5810
DOIs
StatePublished - 1981
Externally publishedYes

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protein phosphorylation
phosphorylation
chloroplasts
energy
wavelengths
polypeptides
peas
pigments
leaves
proteins

ASJC Scopus subject areas

  • General

Cite this

Chloroplast protein phosphorylation couples plastoquinone redox state to distribution of excitation energy between photosystems. / Allen, John F.; Bennett, John; Steinback, Katherine E.; Arntzen, Charles J.

In: Nature, Vol. 291, No. 5810, 1981, p. 25-29.

Research output: Contribution to journalArticle

Allen, John F. ; Bennett, John ; Steinback, Katherine E. ; Arntzen, Charles J. / Chloroplast protein phosphorylation couples plastoquinone redox state to distribution of excitation energy between photosystems. In: Nature. 1981 ; Vol. 291, No. 5810. pp. 25-29.
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