Literature DB >> 139919

Specific photolabelling of beef-heart mitochondrial ATPase by 8-azido-ATP.

R J Wagenvoord, I Van der Kraan, A Kemp.   

Abstract

1. 8-Azido-ATP is a suitable photoaffinity label for beef-heart mitochondrial ATPase (F1) 2. 8-Azido-ATP is hydrolysed slowly by F1 in the dark. Photolysis at 350 nm in the presence of F1 leads to inhibition of the ATPase activity. The presence of ATP during illumination prevents the inhibition. Illumination of F1 in the absence of 8-azido-ATP causes no inhibition. 3. Added Mg2+ is not necessary for the binding of the 8-azido-ATP to F1. 4. 8-Azido-ATP binds specifically to the beta subunits of F1. 5. The ATPase activity is completely inhibited when 2 mol of 8-azido-ATP are bound per mol F1.

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Year:  1977        PMID： 139919     DOI： 10.1016/0005-2728(77)90147-5

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN： 0006-3002


  11 in total

Review 1.  ATP synthase and the actions of inhibitors utilized to study its roles in human health, disease, and other scientific areas.

Authors:  Sangjin Hong; Peter L Pedersen
Journal:  Microbiol Mol Biol Rev       Date:  2008-12       Impact factor: 11.056

2.  Synthesis and properties of 8-azido-1, N6-etheno adenosine triphosphate--a fluorescent and photosensitive ATP analog.

Authors:  H J Schäfer; P Scheurich; G Rathgeber; K Dose
Journal:  Nucleic Acids Res       Date:  1978-04       Impact factor: 16.971

3.  A critical appraisal of evidence for localized energy coupling. Kinetic studies on liposomes containing bacteriorhodopsin and ATP synthase.

Authors:  R L Van der Bend; J Petersen; J A Berden; K Van Dam; H V Westerhoff
Journal:  Biochem J       Date:  1985-09-01       Impact factor: 3.857

Review 4.  Structure and function of proton-translocating adenosine triphosphatase (F0F1): biochemical and molecular biological approaches.

Authors:  M Futai; H Kanazawa
Journal:  Microbiol Rev       Date:  1983-09

5.  Isolation of alpha-subunits of factor F1 from submitochondrial particles and the reconstitution of active ATPase from isolated alpha-subunits and beta-subunits bound to the mitochondrial membrane.

Authors:  I A Kozlov; Y M Milgrom; I S Tsybovski
Journal:  Biochem J       Date:  1980-11-15       Impact factor: 3.857

Review 6.  Recent developments on structural and functional aspects of the F1 sector of H+-linked ATPases.

Authors:  P V Vignais; M Satre
Journal:  Mol Cell Biochem       Date:  1984       Impact factor: 3.396

7.  An active-site-directed adenosine triphosphate analogue binds to the beta-subunits of factor F1 mitochondrial adenosine triphosphatase with its triphosphate moiety.

Authors:  V L Drutsa; I A Kozlov; Y M Milgrom; Z A Shabarova; N I Sokolova
Journal:  Biochem J       Date:  1979-08-15       Impact factor: 3.857

8.  Plastome mutation affecting the chloroplast ATP synthase involves a post-transcriptional defect.

Authors:  B B Sears; R G Herrmann
Journal:  Curr Genet       Date:  1985       Impact factor: 3.886

9.  Study of the rat liver S-adenosylmethionine synthetase active site with 8-azido ATP.

Authors:  H P Deigner; J M Mato; M A Pajares
Journal:  Biochem J       Date:  1995-06-01       Impact factor: 3.857

10.  Effect of phosphate and adenine nucleotides on the rate of labeling of functional groups at the catalytic site of F1-ATPase.

Authors:  L P Ting; J H Wang
Journal:  J Bioenerg Biomembr       Date:  1980-08       Impact factor: 2.945
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