STRUCTURE and FUNCTION OF THE COUPLING‐FACTOR OF PHOTOPHOSPHORYLATION

Galmiche, J. M.; Girault, G.; Lemaire, Claire

doi:10.1111/j.1751-1097.1985.tb03626.x

Cited by 11 publications

(3 citation statements)

References 100 publications

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“…e ATP synthase of chloroplasts is responsible for the photophosphorylation of ADP [cf. Galmiche et al (1985)]. It is similar to other Fi-F0 ATP synthases from mitochondria and bacteria.…”

mentioning

confidence: 66%

Amino acid sequence of the nucleotide binding region of chloroplast coupling factor 1

Admon¹,

Hammes²

1987

Biochemistry

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The labeling of chloroplast coupling factor 1 by 3'-O-(4-benzoyl)benzoyl-ATP (BzATP) was studied. When the enzyme was incubated with approximately 10 microM BzATP and 6 mM MgCl2 at pH 7.9 for approximately 20 min and passed through two Sephadex G-50 centrifuge columns, three BzATP molecules were bound per coupling factor molecule. Photolysis of radioactive enzyme-bound BzATP followed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography revealed that the BzATP bound primarily to the beta-polypeptide. If unbound BzATP was not removed by centrifuge columns prior to photolysis, significant labeling of the alpha-polypeptide also occurred. After photolysis, the BzATP-labeled enzyme was treated with trypsin, and two radioactive peptides were isolated by high-performance liquid chromatography on a C18 column. The two peptides were sequenced and found to correspond to amino acids 360-378 and 393-397 of the beta-polypeptide. For the sequence 360-378, two specific amino acids were found to be radioactive (Tyr-362 and Asp-369). This region of the polypeptide is highly conserved in several different species and probably corresponds to part of the nucleotide binding region of the catalytic site. In the case of amino acids 393-397, a very low level of radioactivity was found for all amino acids. The significance of this peptide for the binding of nucleotides to coupling factor 1 could not be established.

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“…e ATP synthase of chloroplasts is responsible for the photophosphorylation of ADP [cf. Galmiche et al (1985)]. It is similar to other Fi-F0 ATP synthases from mitochondria and bacteria.…”

mentioning

confidence: 66%

Amino acid sequence of the nucleotide binding region of chloroplast coupling factor 1

Admon¹,

Hammes²

1987

Biochemistry

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“…Proton gradients can be either converted into other ionic gradients (23,36) or used for adenosine triphosphate (ATP) production in a mechanism described by the Mitchell chemiosmotic hypothesis (86,163) utilizing an adenosine triphosphatase (76,81).…”

Section: Halobacterium Sppmentioning

confidence: 99%

Photosensory behavior in procaryotes.

Häder¹

1987

Microbiological Reviews

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“…A general background and review of the mitochondrial ATP synthase is provided by Tyler (1984). Valuable reviews of the mitochondrial enzyme are provided by Hatefi (1985) and Vignais and Lunardi (1985); of the Escherichia coli enzyme by Fillingame (1981) and ; of the chloroplast enzyme by Nelson (1981), Strotmann and Bickel-Sandkotter (1984) , Merchant and Selman (1985), and Galmiche et al (1985) ; of the enzyme from different sources by Cross (1981), Amzel and Pedersen (1983), Senior and Wise (1983), and Futai and Kanazawa (1983); and of the F0 portion by Hoppe and Sebald (1984).1 1 References for many statements in this paper will be found in these reviews or furnished by the author on request. Some more recent references are given that will also serve as a guide to the literature.…”

mentioning

confidence: 99%

The unusual enzymology of ATP synthase

Boyer¹

1987

Biochemistry

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STRUCTURE and FUNCTION OF THE COUPLING‐FACTOR OF PHOTOPHOSPHORYLATION

Cited by 11 publications

References 100 publications

Amino acid sequence of the nucleotide binding region of chloroplast coupling factor 1

Amino acid sequence of the nucleotide binding region of chloroplast coupling factor 1

Photosensory behavior in procaryotes.

The unusual enzymology of ATP synthase

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