8-Azido-adenosine 5'-triphosphate as a Photoaffinity Label for Bacterial F1 ATPase
- 1 July 1978
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 88 (1), 253-257
- https://doi.org/10.1111/j.1432-1033.1978.tb12445.x
Abstract
8-Azido-adenosine 5''-triphosphate .**GRAPHIC**. is a suitable photoaffinity label for F1 ATPase [EC 3.6.1.3] from Micrococcus luteus. The nucleotide is a substrate in the presence of bivalent cations and inhibits the enzyme irreversibly upon irradiation with UV light above 300 nm. More than 80% of the label is covalently bound to the .beta. subunits in the presence of bivalent cations. Labeling and inactivation is decreased by protection with ADP, ATP or adenyl-5''-yl imidodiphosphate. To a much smaller degree the .alpha. subunits also become labeled. .**GRAPHIC**. does not specifically bind to the .beta. subunits upon irradiation. Like .**GRAPHIC**. and .**GRAPHIC**. it also labels the .alpha. subunits to a small extent. The F1 ATPase is inactivated after a single .beta. subunit per F1 complex became labeled. A cooperativity of the .beta. subunits carrying nucleotide binding sites is suggested.This publication has 33 references indexed in Scilit:
- F1‐ATPase from Micrococcus sp. ATCC 398European Journal of Biochemistry, 1977
- Photolabeling of the adenine nucleotide carrier by 8-azido-ADPBiochemical and Biophysical Research Communications, 1977
- Interaction of azidonitrophenylaminobutyryl—ADP, a photoaffinity ADP analog, with mitochondrial adenosine triphosphatase. Identification of the labeled subunitsFEBS Letters, 1977
- Kinetic properties of soluble adenosine triphosphatase of escherichia coliMolecular and Cellular Biochemistry, 1977
- Specific photolabelling of beef-heart mitochondrial ATPase by 8-azido-ATPBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1977
- Arylazido aminopropionyl ATP, an active site directed photoaffinity reagent for mitochondrial adenosine triphosphataseBiochemical and Biophysical Research Communications, 1976
- Interaction of the photoaffinity label 8‐azido‐ADP with glutamate dehydrogenaseFEBS Letters, 1976
- Role of Mg2+ ions in the subunit structure and membrane binding properties of bacterial energy transducing ATPaseBiochemical and Biophysical Research Communications, 1976
- Relations between divalent cation binding and ATPase activity in coupling factor from chloroplastFEBS Letters, 1976
- ATPase of Escherichia coli: purification, dissociation, and reconstitution of the active complex from the isolated subunitsBiochemistry, 1976