Spontaneous reactivation of covalently labeled proton adenosinetriphosphatase
- 3 January 1984
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 23 (1) , 136-141
- https://doi.org/10.1021/bi00296a022
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 10 references indexed in Scilit:
- Changes in chemical properties of mitochondrial adenosine triphosphatase upon removal of tightly bound nucleotidesBiochemistry, 1983
- Catalytic site cooperativity of beef heart mitochondrial F1 adenosine triphosphatase. Correlations of initial velocity, bound intermediate, and oxygen exchange measurements with an alternating three-site model.Journal of Biological Chemistry, 1982
- Structure of the mitochondrial F1 ATPase at 9-A resolution.Proceedings of the National Academy of Sciences, 1982
- Catalytic properties of beef heart mitochondrial ATPase modified with 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole. Evidence for catalytic site cooperativity during ATP synthesis.Journal of Biological Chemistry, 1982
- Adenine nucleotide binding sites on beef heart F1-ATPase. Evidence for three exchangeable sites that are distinct from three noncatalytic sites.Journal of Biological Chemistry, 1982
- Reconstitution of oxidative phosphorylation by chemically modified coupling factor F1: differential inhibition of reactions catalyzed by F1 labeled with 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole or 2,3-butanedioneBiochemistry, 1979
- Reversible binding of Pi by beef heart mitochondrial adenosine triphosphatase.Journal of Biological Chemistry, 1977
- An alternating site sequence for oxidative phosphorylation suggested by measurement of substrate binding patterns and exchange reaction inhibitions.Journal of Biological Chemistry, 1977
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976
- PARTIAL RESOLUTION OF ENZYMES CATALYZING OXIDATIVE PHOSPHORYLATION .13. STRUCTURE AND FUNCTION OF SUBMITOCHONDRIAL PARTICLES COMPLETELY RESOLVED WITH RESPECT TO COUPLING FACTOR 11967