Irradiation of the bovine mitochondrial F1-ATPase previously inactivated with 5'-p-fluorosulfonylbenzoyl-8-azido-[3H]adenosine cross-links His-beta 427 to Tyr-beta 345 within the same beta subunit.-Reference-Cited by-同舟云学术

Irradiation of the bovine mitochondrial F1-ATPase previously inactivated with 5'-p-fluorosulfonylbenzoyl-8-azido-[3H]adenosine cross-links His-beta 427 to Tyr-beta 345 within the same beta subunit.

Published:1992-06 Issue:18 Volume:267 Page:12916-12927
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Zhuo S,Garrod S,Miller P,Allison W.S.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference49 articles.

1. ATP SYNTHASE (H+-ATPase): Results by Combined Biochemical and Molecular Biological Approaches

2. ATP synthesis by oxidative phosphorylation

3. Primary structure and subunit stoichiometry of F1-ATPase from bovine mitochondria

4. Interaction of adenine nucleotides with multiple binding sites on beef heart mitochondrial adenosine triphosphatase.

5. The interactions of coupling ATPases with nucleotides

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3. Effect of Nucleotides on the Thermal Stability and on the Deuteration Kinetics of the Thermophilic F0F1 ATP Synthase;European Journal of Biochemistry;1997-03

4. Modification of domains of α and β subunits of F1-ATPase from the thermophylic bacterium PS3, in their isolated and associated forms, by 3′-O-(4-benzoyl)benzoyl adenosine 5′-triphosphate (BzATP);Journal of Bioenergetics and Biomembranes;1996-12

5. 2,8-Diazido-ATP - a short-length bifunctional photoaffinity label for photoaffinity cross-linking of a stable F1in ATP synthase (from thermophilic bacteria PS3);FEBS Letters;1995-12-27