The number and localisation of adenine nucleotide-binding sites in beef-heart mitochondrial ATPase (F1) determined by photolabelling with 8-azido-ATP and 8-azido-ADP-Reference-Cited by-同舟云学术

The number and localisation of adenine nucleotide-binding sites in beef-heart mitochondrial ATPase (F1) determined by photolabelling with 8-azido-ATP and 8-azido-ADP

Published:1980-12 Issue:2 Volume:593 Page:204-211
ISSN:0005-2728
Container-title:Biochimica et Biophysica Acta (BBA) - Bioenergetics
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Bioenergetics

Author:

Wagenvoord R.J.,Kemp A.,Slater E.C.

Publisher

Elsevier BV

Subject

Cell Biology,Biochemistry,Biophysics

Reference31 articles.

1. Partial Resolution of the Enzymes Catalyzing Oxidative Phosphorylation

2. Allosteric influence of anions on mitochondrial ATPase of yeast

3. Kinetic studies on rat liver and beef heart mitochondrial ATPase. Evidence for nucleotide binding at separate regulatory and catalytic sites.

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

5. Localisation of adenine nucleotide-binding sites on beef-heart mitochondrial ATPase by photolabelling with 8-azido-ADP and 8-azido-ATP

Cited by 66 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. 8-N3-3′-Biotinyl-ATP, a Novel Monofunctional Reagent: Differences in the F1- and V1-ATPases by Means of the ATP Analogue;Biochemical and Biophysical Research Communications;2001-09

2. Covalent modification of the catalytic sites of the H+-ATPase from chloroplasts with 2-nitreno-ADP. Modification of the catalytic site 1 (tight) and catalytic sites 1 and 2 together impairs both uni-site and multi-site catalysis of ATP synthesis and ATP hydrolysis;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2000-07

3. Analysis of the nucleotide binding sites of mitochondrial ATP synthase provides evidence for a two-site catalytic mechanism;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2000-05

4. Covalent modification of the catalytic sites of the H+-ATPase from chloroplasts, CF0F1, with 2-azido-[α-32P]ADP: modification of the catalytic site 2 (loose) and the catalytic site 3 (open) impairs multi-site, but not uni-site catalysis of both ATP synthesis and ATP hydrolysis;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2000-01

5. One of the non-exchangeable nucleotides of the mitochondrial F1-ATPase is bound at a β-subunit: evidence for a non-rotatory two-site catalytic mechanism;Biochimica et Biophysica Acta (BBA) - Bioenergetics;1999-06