Catalytic properties of chloroplast F1-ATPase modified at catalytic or noncatalytic sites by 2-azido adenine nucleotides.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference58 articles.
1. Localization of the high-affinity binding site for ATP on the membrane-bound chloroplast ATP synthase.
2. Adenine nucleotide binding sites on beef heart F1 ATPase: photoaffinity labeling of beta-subunit Tyr-368 at a noncatalytic site and beta Tyr-345 at a catalytic site.
3. Catalytic and noncatalytic nucleotide binding sites of chloroplast F1ATPase Photoaffinity labeling and peptide sequencing
4. Catalytic and noncatalytic nucleotide binding sites of theEscherichia coliF1ATPase Amino acid sequences of β-subunit tryptic peptides labeled with 2-azido-ATP
5. Chloroplast F1 ATPase has more than three nucleotide binding sites, and 2-azido-ADP or 2-azido-ATP at both catalytic and noncatalytic sites labels the .beta. subunit
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5. Covalent modification of the non-catalytic sites of the H + -ATPase from chloroplasts with 2-azido-[α- 32 P]ATP and its effect on ATP synthesis and ATP hydrolysis;Biochimica et Biophysica Acta (BBA) - Biomembranes;2001-02
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