Energy Transduction in Chloroplasts: Structure and Function of the ATPase Complex

Shavit, Noun

doi:10.1146/annurev.bi.49.070180.000551

Cited by 117 publications

(32 citation statements)

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“…ref. 1). Chloroplast coupling factor 1 (CF1) is the watersoluble portion of this complex and possesses a latent ATPase activity specific for Ca2+ (2).…”

mentioning

confidence: 99%

Investigation of nucleotide binding sites on chloroplast coupling factor 1 with 3'O-(4-benzoyl)benzoyl adenosine 5'-triphosphate.

Kambouris¹,

Hammes²

1985

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

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The subunit locations of each of the three nucleotide binding sites of soluble chloroplast coupling factor 1 have been studied with the photoaffinity label 3'-O-(4-benzoyl)benzoyl-ATP. This derivative is an effective inhibitor of ATPase activity. Photolysis of the radioactive label when bound to each of the three nucleotide sites on the coupling factor has been examined. For the nucleotide site that normally binds ADP very tightly, NaDodSO4/polyacrylamide gel electrophoresis after photolysis indicates that primarily the beta polypeptide chain is appreciably labeled (86%), although some labeling of the alpha polypeptide chain is found (14%). For the site that binds MgATP tightly, 97% of the radioactivity is found on the beta polypeptide chain. The alpha and beta polypeptide chains are labeled in approximately equal amounts when photolysis is carried out with the nucleotide analog bound to the third site.

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“…ref. 1). Chloroplast coupling factor 1 (CF1) is the watersoluble portion of this complex and possesses a latent ATPase activity specific for Ca2+ (2).…”

mentioning

confidence: 99%

Investigation of nucleotide binding sites on chloroplast coupling factor 1 with 3'O-(4-benzoyl)benzoyl adenosine 5'-triphosphate.

Kambouris¹,

Hammes²

1985

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

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“…The iodinated protein A was collected in the void volume after passage through a Sephadex G-50 column (in a 1 ml tuberculin syringe). A specific activity of [1][2][3][4][5][6][7][8][9][10] ,&Ci/,ug was obtained.…”

mentioning

confidence: 99%

A M _r 95,000 polypeptide in Porphyridium cruentum phycobilisomes and thylakoids: Possible function in linkage of phycobilisomes to thylakoids and in energy transfer

Redlinger

Gantt

1982

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

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Two pigmented polypeptides with the same molecular weight (Mr 95,000) were isolated from the photosynthetic apparatus of Porphyridium cruentum by sodium dodecyl sulfate/ polyacrylamide gel electrophoresis. A blue polypeptide from phycobilisomes had absorption and fluorescence emission spectra similar to those of allophycocyanin. A green-pigmented polypeptide from photosynthetic membranes (free of phycobilisomes) contained chlorophyll a. Several properties were common to the Mr 95,000 polypeptides from both sources: (i) identical molecular weights, (ii) identical gel electrophoresis patterns after limited protease digestion, and (iii) immunological crossreactivity with an IgG fraction directed against the Mr 95,000 polypeptide from phycobilisomes. On the basis of this evidence, a common polypeptide exists in phycobilisomes and thylakoids, and it probably anchors the phycobilisome to the thylakoid membrane. The fluorescence emission overlap of the blue and green polypeptides suggests that they are involved in the transfer of energy from phycobilisomes to thylakoids.Phycobilisomes are organelles on the photosynthetic membrane of red and blue-green algae (cyanobacteria) that function in absorbing light in the wavelength region where chlorophyll absorption is low. Such an extension of the absorption region especially benefits organisms growing under light-limiting conditions. Light absorbed by the phycobiliproteins (phycoerythrin, phycocyanin, and allophycocyanin) is funnelled through a long-wavelength-emitting allophycocyanin to chlorophyll a (reviewed in ref. 1). In cells ofthe red alga Porphyridium cruentum, Duysens (2) and French and Young (3) demonstrated energy transfer from phycoerythrin to chlorophyll. Because the transfer efficiencies from phycobiliproteins to chlorophyll are high (80-90%), it is expected that phycobilisomes have a functional attachment site in close proximity to photosynthetic reaction centers (4). Although phycobilisome attachment molecule(s) have not yet been found, such molecules have been identified for another thylakoid binding complex, the coupling factor (5). Assuming that there are specific attachment molecule(s) in phycobilisomes, we have undertaken a comparison of the polypeptide compositions of isolated phycobilisomes and of thylakoids (free of phycobilisomes) to determine which components are likely to be involved in phycobilisome/thylakoid attachment and energy transfer.The phycobilisome protein composition ofP. cruentum (synonymous with P. purpureum) has been reported (6). As with many other algae (7-9), the phycobilisomes were found to consist of many polypeptides, some ofwhich appeared colored and others noncolored after NaDodSO4/polyacrylamide gel electrophoresis. A pigmented polypeptide (F680) was reported to have a high molecular weight (95,000) and to constitute approximately 1.3% of the phycobilisome protein on the basis of Coomassie blue staining (6). As already reported in a preliminary communication (10), a polypeptide with the same molecular weight and a si...

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“…Chlorophyll content was estimated according to [16]. [14]. 32Piincorporated or liberated were determined by the isobutanol benzene extraction method [ 171.…”

Section: Methodsmentioning

confidence: 99%

Role of tight nucleotide binding in the regulation of the chloroplast ATP synthetase activities

Bar-Zvi¹,

Shavit²

1980

FEBS Letters

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Energy Transduction in Chloroplasts: Structure and Function of the ATPase Complex

Cited by 117 publications

References 0 publications

Investigation of nucleotide binding sites on chloroplast coupling factor 1 with 3'O-(4-benzoyl)benzoyl adenosine 5'-triphosphate.

Investigation of nucleotide binding sites on chloroplast coupling factor 1 with 3'O-(4-benzoyl)benzoyl adenosine 5'-triphosphate.

A M _r 95,000 polypeptide in Porphyridium cruentum phycobilisomes and thylakoids: Possible function in linkage of phycobilisomes to thylakoids and in energy transfer

Role of tight nucleotide binding in the regulation of the chloroplast ATP synthetase activities

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Energy Transduction in Chloroplasts: Structure and Function of the ATPase Complex

Cited by 117 publications

References 0 publications

Investigation of nucleotide binding sites on chloroplast coupling factor 1 with 3'O-(4-benzoyl)benzoyl adenosine 5'-triphosphate.

Investigation of nucleotide binding sites on chloroplast coupling factor 1 with 3'O-(4-benzoyl)benzoyl adenosine 5'-triphosphate.

A M r 95,000 polypeptide in Porphyridium cruentum phycobilisomes and thylakoids: Possible function in linkage of phycobilisomes to thylakoids and in energy transfer

Role of tight nucleotide binding in the regulation of the chloroplast ATP synthetase activities

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A M _r 95,000 polypeptide in Porphyridium cruentum phycobilisomes and thylakoids: Possible function in linkage of phycobilisomes to thylakoids and in energy transfer