Assessment of the rate of bound substrate interconversion and of ATP acceleration of product release during catalysis by mitochondrial adenosine triphosphatase.-Reference-Cited by-同舟云学术

Assessment of the rate of bound substrate interconversion and of ATP acceleration of product release during catalysis by mitochondrial adenosine triphosphatase.

Published:1984-05 Issue:9 Volume:259 Page:5761-5767
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

O'Neal C C,Boyer P D

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference47 articles.

1. 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.

2. Assessment of total catalytic sites and the nature of bound nucleotide participation in photophosphorylation.

3. Mitochondrial-catalyzed ATP hydrolysis in highly enriched [18O]H2O.

4. Occurrence and significance of oxygen exchange reactions catalyzed by mitochondrial adenosine triphosphatase preparations.

5. Subunit interaction during catalysis. Alternating site cooperativity of mitochondrial adenosine triphosphatase.

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