Photolabeling of the phosphate binding site of mitochondrial F1-ATPase by [32P]azidonitrophenyl phosphate. Identification of the photolabeled amino acid residues
[32P]Azidonitrophenyl phosphate [( 32P]ANPP) is a photoactivatable analogue of Pi. It competes efficiently with Pi for binding to the F1 sector of beef heart mitochondrial ATPase and photolabels the Pi binding site located in the beta subunit of F1 [Lauquin, G. J. M., Pougeois, R., & Vignais, P. V. (1980) Biochemistry 19, 4620-4626]. By cleavage of the photolabeled beta subunit of F1 with cyanogen bromide, trypsin, and chymotrypsin, bound [32P]ANPP was localized in a fragment spanning Thr 299-Phe 326. By Edman degradation of the radiolabeled tryptic peptide spanning Ile 296-Arg 337, [32P]ANPP was found to be attached covalently by its photoreactive group to Ile 304, Gln 308, and Tyr 311. These results are discussed in terms of a model in which the phosphate group of [32P]ANPP interacts with a glycine-rich sequence of the beta subunit, spanning Gly 156-Lys 162, which is spatially close to the photolabeled Ile 304-Tyr 311 segment of the same subunit.
Medienart: |
Artikel |
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Erscheinungsjahr: |
1989 |
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Erschienen: |
1989 |
Enthalten in: |
Zur Gesamtaufnahme - volume:28 |
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Enthalten in: |
Biochemistry - 28(1989), 4 vom: 21. Feb., Seite 1442-8 |
Sprache: |
Englisch |
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Beteiligte Personen: |
Garin, J [VerfasserIn] |
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Anmerkungen: |
Date Completed 27.06.1989 Date Revised 13.06.2019 published: Print Citation Status MEDLINE |
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Förderinstitution / Projekttitel: |
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PPN (Katalog-ID): |
NLM025055992 |
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100 | 1 | |a Garin, J |e verfasserin |4 aut | |
245 | 1 | 0 | |a Photolabeling of the phosphate binding site of mitochondrial F1-ATPase by [32P]azidonitrophenyl phosphate. Identification of the photolabeled amino acid residues |
264 | 1 | |c 1989 | |
336 | |a Text |b txt |2 rdacontent | ||
337 | |a ohne Hilfsmittel zu benutzen |b n |2 rdamedia | ||
338 | |a Band |b nc |2 rdacarrier | ||
500 | |a Date Completed 27.06.1989 | ||
500 | |a Date Revised 13.06.2019 | ||
500 | |a published: Print | ||
500 | |a Citation Status MEDLINE | ||
520 | |a [32P]Azidonitrophenyl phosphate [( 32P]ANPP) is a photoactivatable analogue of Pi. It competes efficiently with Pi for binding to the F1 sector of beef heart mitochondrial ATPase and photolabels the Pi binding site located in the beta subunit of F1 [Lauquin, G. J. M., Pougeois, R., & Vignais, P. V. (1980) Biochemistry 19, 4620-4626]. By cleavage of the photolabeled beta subunit of F1 with cyanogen bromide, trypsin, and chymotrypsin, bound [32P]ANPP was localized in a fragment spanning Thr 299-Phe 326. By Edman degradation of the radiolabeled tryptic peptide spanning Ile 296-Arg 337, [32P]ANPP was found to be attached covalently by its photoreactive group to Ile 304, Gln 308, and Tyr 311. These results are discussed in terms of a model in which the phosphate group of [32P]ANPP interacts with a glycine-rich sequence of the beta subunit, spanning Gly 156-Lys 162, which is spatially close to the photolabeled Ile 304-Tyr 311 segment of the same subunit | ||
650 | 4 | |a Journal Article | |
650 | 4 | |a Research Support, Non-U.S. Gov't | |
650 | 7 | |a Affinity Labels |2 NLM | |
650 | 7 | |a Azides |2 NLM | |
650 | 7 | |a Macromolecular Substances |2 NLM | |
650 | 7 | |a Phosphorus Radioisotopes |2 NLM | |
650 | 7 | |a 4-azido-2-nitrophenyl phosphate |2 NLM | |
650 | 7 | |a 74784-75-1 |2 NLM | |
650 | 7 | |a Proton-Translocating ATPases |2 NLM | |
650 | 7 | |a EC 3.6.3.14 |2 NLM | |
700 | 1 | |a Michel, L |e verfasserin |4 aut | |
700 | 1 | |a Dupuis, A |e verfasserin |4 aut | |
700 | 1 | |a Issartel, J P |e verfasserin |4 aut | |
700 | 1 | |a Lunardi, J |e verfasserin |4 aut | |
700 | 1 | |a Hoppe, J |e verfasserin |4 aut | |
700 | 1 | |a Vignais, P |e verfasserin |4 aut | |
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