Specific placement of tryptophan in the catalytic sites of Escherichia coli F1-ATPase provides a direct probe of nucleotide binding: maximal ATP hydrolysis occurs with three sites occupied.-Reference-Cited by-同舟云学术

Specific placement of tryptophan in the catalytic sites of Escherichia coli F1-ATPase provides a direct probe of nucleotide binding: maximal ATP hydrolysis occurs with three sites occupied.

Published:1993-09 Issue:27 Volume:268 Page:20126-20133
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Weber J,Wilke-Mounts S,Lee R.S.,Grell E,Senior A.E.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference49 articles.

1. Amino acid sequence of the nucleotide binding region of chloroplast coupling factor 1

2. Catalytic sites of Escherichia coli F1-ATPase. Characterization of unisite catalysis at varied pH

3. Directed mutagenesis of the strongly conserved aspartate 242 in the beta-subunit of Escherichia coli proton-ATPase.

4. Functional sites in F1-ATPases: Location and interactions

5. Suggestions for “safe” residue substitutions in site-directed mutagenesis

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