Uni‐site catalysis by Escherichia coli F1‐ATPase with different numbers of bound nucleotides
- 6 November 1989
- journal article
- Published by Wiley in FEBS Letters
- Vol. 257 (2) , 465-467
- https://doi.org/10.1016/0014-5793(89)81597-2
Abstract
We prepared two types of E. coli F1 by slightly different gel filtration procedures of the purified F1: F1(II) contained about 2 mol, and F1(V) about 5 mol of bound adenine nucleotides per mol of the enzyme. Thus F1(II) had more than 2, possibly 3, vacant catalytic sites, while F1(V) had less than one vacant catalytic site. The rate of ATP hydrolysis in uni‐site catalysis (in the presence of inorganic phosphate) was about 3‐fold higher with F1(II) than with F1(V), suggesting that ADP and inorganic phosphate bound at the catalytic sites of F1(V) changed the kinetics of uni‐site catalysis significantly.Keywords
This publication has 19 references indexed in Scilit:
- ATP SYNTHASE (H+-ATPase): Results by Combined Biochemical and Molecular Biological ApproachesAnnual Review of Biochemistry, 1989
- Characterization of exchangeable and nonexchangeable bound adenine nucleotides in F1-ATPase from Escherichia coli.Journal of Biological Chemistry, 1986
- Photoaffinity labeling of mitochondrial adenosine triphosphatase by [.alpha.-32P]2-azido ADPBiochemistry, 1985
- Measurement of protein using bicinchoninic acidAnalytical Biochemistry, 1985
- Chapter 8 The Proton-ATPase of Escherichia coliPublished by Elsevier ,1985
- Specificity of the proton adenosine triphosphatase of Escherichia coli for adenine, guanine, and inosine nucleotides in catalysts and bindingBiochemistry, 1984
- The UNC operon nucleotide sequence, regulation and structure of ATP-synthaseBiochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1984
- Properties of F1-ATPase from the uncD412 mutant of Escherichia coliBiochemical Journal, 1983
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Purification and Properties of Reconstitutively Active and Inactive Adenosinetriphosphatase from Escherichia coliProceedings of the National Academy of Sciences, 1974