Excitation energy transfer in the light-harvesting chlorophyll ab · protein

Metter, Richard L. Van

doi:10.1016/0005-2728(77)90107-4

Cited by 85 publications

(44 citation statements)

References 25 publications

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“…It has been assumed in these calculations that all of the component polypeptides of LHCII bind Chl equally. Spectroscopic data have indicated that Chl b molecules in LHCII monomers are oriented around a three-fold symmetry axis (13,28,30). This means that the Chl b molecules are either organized in multiples of three, or that there are three Chl b molecules around a threefold symmetry axis plus two or three separately organized Chl b molecules.…”

Section: Discussionmentioning

confidence: 99%

“…Thus the peak at 674 nm has been alternatively attributed to Chl a (8) or to exciton splitting due to interactions between Chl b trimers (13,28,30). The latter model was based on spectra of monomeric LHCII isolated by preparative SDS-PAGE, where the CD signals due to Chl a were nearly non-existent.…”

Section: Discussionmentioning

confidence: 99%

“…Excitation energy transfer between Chl molecules occurs with almost 100% efficiency within the complex and the pigments are protected against contact with the aqueous environment by the folding of the polypeptide chain (29). Circular dichroism spectra in the visible range suggested that the Chl b molecules in LHCII isolated by preparative SDS-PAGE were arranged round a three-fold symmetry axis (28,30).…”

Section: U G Hinz and Ic G Welinder: Structure And Chlorophyll Organmentioning

confidence: 99%

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The light-harvesting complex of photosystem II in barley. Structure and chlorophyll organization

Hinz

Welinder

1987

Carlsberg Res. Commun.

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The isolated light-harvesting complex of photosystem II (LHCII) in barley had a chlorophyll (Chl) a/b ratio of 1.37 (mol/mol) and contained an average of 13.1 Chl molecules per 25 kD polypeptide chain, corresponding to 7.6 molecules of Chl a and 5.5 molecules of Chl b. Tryptic digestion of native LHCII yielded a 16 kD fragment which contained 12 of these 13 Chl molecules. The 16 kD fragment started with the serine 52 of the mature polypeptide, as determined by N-terminal amino acid sequence analysis and comparison with the amino acid sequence deduced from the nucleotide sequence of a corresponding gene in wheat (LAMPPA et al. 1985). Circular dichroism measurements of LHCII in 1% SDS or at extremes ofpH, showed that there were at least two populations ofChl a and that Chl a was much more sensitive to changes in the aqueous environment than Chl b. We present a model for the folding of LHCII with four transmembrane helices, based on the above results and on the application of the rules of CHou and FASMAN ( 1978 ) and PAUL and ROSENBUSCH ( 1985) for the prediction of secondary structure using the wheat sequence.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: U G Hinz and Ic G Welinder: Structure And Chlorophyll Organmentioning

confidence: 99%

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The light-harvesting complex of photosystem II in barley. Structure and chlorophyll organization

Hinz

Welinder

1987

Carlsberg Res. Commun.

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“…On the basis of absorption, circular dichroism, and fluorescence polarization, a model of the relative chromophore orientations in the Chl a/bprotein has been developed [6][7][8]12] Fig. 1.…”

Section: Statement Of the Problemmentioning

confidence: 99%

“…Knox, Department of Physics and Astronomy, University of Rochester, Rochester, NY 14627-0011, USA contain three Chi a, three Chi b, and one carotenoid molecule [4] having a total molecular mass of 30 kDa [1,5]. Because of its small number of chromophores, CP:II has received more attention theoretically, and a model involving a trimer of Chl b has been developed based on spectral studies [6][7][8]. Although LHC-II particles are more complicated than CP-II, they have many similar features.…”

Section: Introductionmentioning

confidence: 99%

Applications of a CP‐II model to excitation transfer experiments on light‐harvesting chlorophylla/b‐protein complexes

Lin

Knox

1988

FEBS Letters

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A theoretical study of energy-transfer rates between chlorophyll a molecules within light-harvesting chlorophyll a/b complexes of photosystem II (LHC-II) based on transient absorption recovery data [(1985) FEBS Lett. 193, 267-270] has been made using a trimer model of interacting chromophores [(1977) Biochim. Biophys. Acta 462, 642-658]. It provides a kinetic explanation of the data and shows that the experimental results on LHC-II are consistent with and therefore support the model.

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Transfer and Trapping of Excitation Energy in Photosystem II

Duysens

1979

Novartis Foundation Symposia

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Excitation energy transfer in the light-harvesting chlorophyll ab · protein

Cited by 85 publications

References 25 publications

The light-harvesting complex of photosystem II in barley. Structure and chlorophyll organization

The light-harvesting complex of photosystem II in barley. Structure and chlorophyll organization

Applications of a CP‐II model to excitation transfer experiments on light‐harvesting chlorophylla/b‐protein complexes

Transfer and Trapping of Excitation Energy in Photosystem II

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