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

doi:10.1038/291025a0

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

Arizona State University

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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 language	English (US)
Pages (from-to)	25-29
Number of pages	5
Journal	Nature
Volume	291
Issue number	5810
DOIs	https://doi.org/10.1038/291025a0
State	Published - Dec 1 1981

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title = "Chloroplast protein phosphorylation couples plastoquinone redox state to distribution of excitation energy between photosystems",

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.",

author = "Allen, {John F.} and John Bennett and Steinback, {Katherine E.} and Arntzen, {Charles J.}",

year = "1981",

month = dec,

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doi = "10.1038/291025a0",

language = "English (US)",

volume = "291",

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journal = "Nature",

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T1 - Chloroplast protein phosphorylation couples plastoquinone redox state to distribution of excitation energy between photosystems

AU - Allen, John F.

AU - Bennett, John

AU - Steinback, Katherine E.

AU - Arntzen, Charles J.

PY - 1981/12/1

Y1 - 1981/12/1

N2 - 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.

AB - 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.

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

Abstract

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