A voltage-dependent chloride channel in the photosynthetic membrane of a higher plant

Schönknecht, Gerald; Hedrich, Rainer; Junge, Wolfgang; Raschke, Klaus

doi:10.1038/336589a0

Cited by 116 publications

(68 citation statements)

References 15 publications

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“…Cu 21 transport activity across the thylakoid membranes appears to be unaffected by a pH gradient, indicating a lack of proton-linked activity. In addition, we would not expect there to be much of a potential gradient effect due to the presence of a chloride channel in this membrane (Schonknecht et al, 1988).…”

Section: Discussionmentioning

confidence: 99%

Copper Transport Across Pea Thylakoid Membranes

2004

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The initial rate of Cu2+ movement across the thylakoid membrane of pea (Pisum sativum) chloroplasts was directly measured by stopped-flow spectrofluorometry using membranes loaded with the Cu2+-sensitive fluorophore Phen Green SK. Cu2+ transport was rapid, reaching completion within 0.5 s. The initial rate of uptake was dependent upon Cu2+ concentration and saturated at about 0.6 μm total Cu2+. Cu2+ uptake was maximal at a thylakoid lumen pH of 7.0. Cu2+ transport was inhibited by Zn2+ but was largely unaffected by Mn2+ and Cu+. Zn2+ inhibited Cu2+ transport to a maximum of 60%, indicating that there may be more than one transporter for copper in pea thylakoid membranes

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Section: Discussionmentioning

confidence: 99%

Copper Transport Across Pea Thylakoid Membranes

2004

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“…Parenthetically, this question can be placed in the more general context of the as-yet ill-defined role of ion channels recently discovered in other subcellular organelles (Hedrich et al, 1986;Keller et al, 1988a;Rahamimoff et aI., 1988;Schoenknecht et al, 1988).…”

Section: Discussionmentioning

confidence: 99%

“…For instance, it has been possible to detect, at the molecular level, highly conductive ion channels in vacuoles (Hedrich et al, 1986), in the thylakoid membrane of plant cells (Schoenknecht et al, 1988), and in the sarcoplasmic reticulum of frog muscle fibers (Stein and Palade, 1988). By enlarging purified membranes, in order to obtain vesicles large enough to be patch clamped, ion channels have also been found in synaptic vesicles (Rahamimoffet aI., 1988) and in endoplasmic reticulum (Keller et aI., 1988a).…”

Section: Introductionmentioning

confidence: 99%

Further investigation on the high-conductance ion channel of the inner membrane of mitochondria

Sorgato

Morán

Pinto

et al. 1989

J Bioenerg Biomembr

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By use of the patch-clamp technique, the inner membrane of mouse liver and heart mitochondria is shown to contain a highly conductive (around t00 pS in symmetrical 150 mM KC1) and voltage-dependent ion channel. This channel closely resembles that previously found in cuprizone-treated mouse liver inner mitochondrial membrane. The paper discusses the electrical properties of the channel and its possible physiological function. The reconstitution in giant liposomes of a partially purified ox heart inner membrane fraction containing the channel and the use of various inhibitors are also presented.

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“…31). These channels appear to be voltage gated (32), which raises the possibility that illumination leads to a proton motive force-controlled swelling of the lumen by chloride influx.…”

Section: And References Therein)mentioning

confidence: 99%

Dynamic control of protein diffusion within the granal thylakoid lumen

Kirchhoff

Hall

Wood

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

219

224

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The machinery that conducts the light-driven reactions of oxygenic photosynthesis is hosted within specialized paired membranes called thylakoids. In higher plants, the thylakoids are segregated into two morphological and functional domains called grana and stroma lamellae. A large fraction of the luminal volume of the granal thylakoids is occupied by the oxygen-evolving complex of photosystem II. Electron microscopy data we obtained on dark-and light-adapted Arabidopsis thylakoids indicate that the granal thylakoid lumen significantly expands in the light. Models generated for the organization of the oxygen-evolving complex within the granal lumen predict that the light-induced expansion greatly alleviates restrictions imposed on protein diffusion in this compartment in the dark. Experiments monitoring the redox kinetics of the luminal electron carrier plastocyanin support this prediction. The impact of the increase in protein mobility within the granal luminal compartment in the light on photosynthetic electron transport rates and processes associated with the repair of photodamaged photosystem II complexes is discussed.T he primary processes of photosynthesis in cyanobacteria, algae, and higher plants are carried out within flattened vesicles, called thylakoids, which host the molecular complexes that conduct the light-driven reactions of photosynthesis and provide a medium for energy transduction. In higher plants and some green algae, the thylakoids are differentiated into two distinct morphological domains: cylindrical stacked regions ranging between 300 and 600 nm in diameter, coined grana, and unstacked membrane regions that interconnect the grana called stroma lamellae. The photosynthetic protein complexes are unevenly distributed between the two domains: most of photosystem II (PSII) and the major light-harvesting antenna complex II (LHCII) are localized in the appressed regions of the grana, whereas photosystem I (PSI) and ATP synthase are confined to nonappressed membrane regions, which include the stroma lamellae and grana end membranes and margins (refs. 1-4 and references therein).The current study focuses on the thylakoid luminal compartment. This compartment forms a continuous aqueous space encased by the thylakoid membranes, which separate it from the chloroplast stroma. The major inhabitant of the thylakoid lumen in the granal membrane domains is the oxygen-evolving complex (OEC), which stabilizes the manganese catalytic center of PSII and optimizes the ionic environment for water oxidation (ref. 5 and references therein). The very high density of PSII in the granal membranes (6) implies that the space available for movement in the lumen of these thylakoids may be limited, depending on the thickness of this compartment. This impending constraint, in turn, raises the possibility that diffusion of proteins in the granal thylakoid lumen may be modulated by reversible changes in its thickness. Such changes may occur in response to alterations in the light environment. To test this possibility, we ...

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A voltage-dependent chloride channel in the photosynthetic membrane of a higher plant

Cited by 116 publications

References 15 publications

Copper Transport Across Pea Thylakoid Membranes

Copper Transport Across Pea Thylakoid Membranes

Further investigation on the high-conductance ion channel of the inner membrane of mitochondria

Dynamic control of protein diffusion within the granal thylakoid lumen

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