Interaction of nucleotide-depleted F1-ATPase with ADP
- 31 May 1989
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Bioenergetics
- Vol. 975 (1), 50-58
- https://doi.org/10.1016/s0005-2728(89)80200-2
Abstract
No abstract availableKeywords
This publication has 65 references indexed in Scilit:
- The complex of mitochondrial F1‐ATPase with the natural inhibitor protein is unable to catalyze single‐site ATP hydrolysisFEBS Letters, 1988
- Site-directed mutagenesis of stable adenosine triphosphate synthaseBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1988
- On the rate of F1‐ATPase turnover during ATP hydrolysis by the single catalytic site Evidence that hydrolysis with a slow rate of product release does not occur at the alternating active siteFEBS Letters, 1987
- Steady‐state rate of F1‐ATPase turnover during ATP hydrolysis by the single catalytic siteFEBS Letters, 1987
- Total number and differentiation of nucleotide binding sites on mitochondrial F1‐ATPaseEuropean Journal of Biochemistry, 1985
- Tightly bound adenosine diphosphate, which inhibits the activity of mitochondrial F1‐ATPase, is located at the catalytic site of the enzymeFEBS Letters, 1985
- The proton-ATPase of bacteria and mitochondriaThe Journal of Membrane Biology, 1983
- The interactions of coupling ATPases with nucleotidesBiochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1978
- H+-adenosine triphosphatase and membrane energy couplingBiochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1977
- Active/inactive state transitions of mitochondrial ATPase molecules influenced by Mg2+, anions and aurovertinFEBS Letters, 1975