ATP Synthesis by F0F1-ATP Synthase Independent of Noncatalytic Nucleotide Binding Sites and Insensitive to Azide Inhibition-Reference-Cited by-同舟云学术

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ATP Synthesis by F0F1-ATP Synthase Independent of Noncatalytic Nucleotide Binding Sites and Insensitive to Azide Inhibition

Published:1998-01 Issue:2 Volume:273 Page:865-870
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Bald Dirk,Amano Toyoki,Muneyuki Eiro,Pitard Bruno,Rigaud Jean-Louis,Kruip Jochen,Hisabori Toru,Yoshida Masasuke,Shibata Masaki

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference34 articles.

1. THE ATP SYNTHASE—A SPLENDID MOLECULAR MACHINE

2. Catalytic mechanism of F1-ATPase

3. Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria

4. Rotation of subunits during catalysis by Escherichia coli F1-ATPase.

5. Intersubunit rotation in active F-ATPase

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4. 1,5-disubstituted-1,2,3-triazoles counteract mitochondrial dysfunction acting on F1FO-ATPase in models of cardiovascular diseases;Pharmacological Research;2023-01

5. Bottom-Up Synthetic Biology Using Cell-Free Protein Synthesis;Cell-free Macromolecular Synthesis;2023

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