Escherichia coli F1 ATPase is reversibly inhibited by intra- and intersubunit crosslinking: an approach to assess rotational catalysis
- 1 January 1987
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Bioenergetics
- Vol. 890 (1), 97-105
- https://doi.org/10.1016/0005-2728(87)90073-9
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- Thiol modification as a probe of conformational forms of the F1 ATPase of Escherichia coli and of the structural asymmetry of its beta subunitsEuropean Journal of Biochemistry, 1986
- Molecular mechanics of protonmotive F0F1 ATPasesFEBS Letters, 1985
- Hypothesis the mecanism of ATP synthase conformational change by rotation of the b-subunitBiochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1984
- The UNC operon nucleotide sequence, regulation and structure of ATP-synthaseBiochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1984
- Structural asymmetry of the F1 of Escherichiacoli as indicated by reaction with dicyclohexylcarbodiimideBiochemical and Biophysical Research Communications, 1984
- A Loose Coupling Mechanism of Synthesis of ATP by Proton Flux in the Molecular Machine of Living CellsJournal of the Physics Society Japan, 1984
- The proton-ATPase of bacteria and mitochondriaThe Journal of Membrane Biology, 1983
- Structure and function of proton-translocating adenosine triphosphatase (F0F1): biochemical and molecular biological approaches.Microbiological Reviews, 1983
- The Mechanism and Regulation of ATP Synthesis by F1-ATPasesAnnual Review of Biochemistry, 1981
- Subunit composition, function, and spatial arrangement in the Ca2+- and Mg2+-activated adenosine triphosphatases of Escherichia coli and Salmonella typhimuriumArchives of Biochemistry and Biophysics, 1975