Combined application of site-directed mutagenesis, 2-azido-ATP labeling, and lin-benzo-ATP binding to study the noncatalytic sites of Escherichia coli F1-ATPase.-Reference-Cited by-同舟云学术

Combined application of site-directed mutagenesis, 2-azido-ATP labeling, and lin-benzo-ATP binding to study the noncatalytic sites of Escherichia coli F1-ATPase.

Published:1993-03 Issue:9 Volume:268 Page:6241-6247
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

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

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference56 articles.

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

2. The unusual enzymology of ATP synthase

3. A perspective of the binding change mechanism for ATP synthesis 1

4. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

5. On the location and function of the noncatalytic sites on the bovine heart mitochondrial F1-ATPase.

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