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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
44
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pubmed:dateCreated |
1993-12-16
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pubmed:abstractText |
The lateral migration of the integral light-harvesting chlorophyll a/b protein complex of photosystem II, LHCII, has been studied in the undisturbed membranes of thylakoids without artificial probes. LHCII was phosphorylated at 0 degree C. The diffusion of the mobile phospho-LHCII from appressed grana to nonappressed membrane regions was induced by a temperature jump to 20 degrees C and analyzed by a rapid detergent fractionation of the two membrane areas. This long-range diffusion of the integral phospho-LHCII is analyzed by a Monte Carlo calculation which is based on a model of the thylakoid membrane and includes all integral proteins as mobile particles. A comparison of the calculation with the experimental time course indicates a diffusion constant of phospho-LHCII in the range of (2-4) x 10(-12) cm2 s-1. This value is evidence for a severe restriction of protein mobility in the appressed thylakoid membrane. From a statical point of view, the percolation theory predicts that the high protein density in the grana membranes is above the threshold of percolation and the long-range diffusion should be inhibited by finite clusters of lipids. However, the shape of the experimental time course is in favor of a lateral motion also of photosystem II and nonphosphorylated LHCII and not of a rigid lattice of these complexes. Our data and Monte Carlo analysis suggest a dynamic or fluid lattice of the protein complexes with a lifetime of the clusters in the millisecond time range. The consequences of these transient fluctuations on the long-range diffusion of plastoquinone are discussed.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Light-Harvesting Protein Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Photosynthetic Reaction Center...,
http://linkedlifedata.com/resource/pubmed/chemical/Photosystem II Protein Complex
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
9
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pubmed:volume |
32
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
11915-22
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8218264-Adenosine Triphosphate,
pubmed-meshheading:8218264-Algorithms,
pubmed-meshheading:8218264-Diffusion,
pubmed-meshheading:8218264-Kinetics,
pubmed-meshheading:8218264-Light-Harvesting Protein Complexes,
pubmed-meshheading:8218264-Macromolecular Substances,
pubmed-meshheading:8218264-Models, Biological,
pubmed-meshheading:8218264-Models, Structural,
pubmed-meshheading:8218264-Monte Carlo Method,
pubmed-meshheading:8218264-Photosynthetic Reaction Center Complex Proteins,
pubmed-meshheading:8218264-Photosystem II Protein Complex,
pubmed-meshheading:8218264-Plants,
pubmed-meshheading:8218264-Time Factors
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pubmed:year |
1993
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pubmed:articleTitle |
Lateral diffusion of an integral membrane protein: Monte Carlo analysis of the migration of phosphorylated light-harvesting complex II in the thylakoid membrane.
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pubmed:affiliation |
Lehrstuhl für Biochemie der Pflanzen, Albert-Ludwigs-Universität, Freiburg, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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