The ADP that binds tightly to nucleotide-depleted mitochondrial F1-ATPase and inhibits catalysis is bound at a catalytic site
- 1 October 1990
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Bioenergetics
- Vol. 1020 (1) , 43-48
- https://doi.org/10.1016/0005-2728(90)90091-h
Abstract
No abstract availableKeywords
This publication has 41 references indexed in Scilit:
- Interaction of nucleotide-depleted F1-ATPase with ADPBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1989
- Relationship of tightly bound ADP and ATP to control and catalysis by chloroplast ATP synthaseBiochemistry, 1988
- Single-Site Catalysis of F1-ATPase from Thennophilic Bacterium PS3 and Its Dominance in Steady-State Catalysis at Low ATP Concentration1The Journal of Biochemistry, 1987
- Steady‐state rate of F1‐ATPase turnover during ATP hydrolysis by the single catalytic siteFEBS Letters, 1987
- Tightly bound adenosine diphosphate, which inhibits the activity of mitochondrial F1‐ATPase, is located at the catalytic site of the enzymeFEBS Letters, 1985
- Interaction of Mg+2 with beef heart mitochondrial ATPase (F1)Biochemical and Biophysical Research Communications, 1979
- An inhibitory high affinity binding site for ADP in the oligomycin-sensitive ATPase of beef heart submitochondrial particlesBiochemical and Biophysical Research Communications, 1979
- Control of kinetic changes in ATPase activity of soluble coupling factor 1 from chloroplastsFEBS Letters, 1978
- Active/inactive state transitions of mitochondrial ATPase molecules influenced by Mg2+, anions and aurovertinFEBS Letters, 1975
- Adenosine Triphosphatase from Rat Liver MitochondriaPublished by Elsevier ,1972