Distribution of [18O]Pi species from [gamma-18O]ATP hydrolysis by myosin and heavy meromyosin. Evidence for two kinds of myosin-active site differing in their rate of intermediate oxygen exchange.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference33 articles.
1. Mechanism of oxygen exchange in actin-activated hydrolysis of adenosine triphosphate by myosin subfragment 1
2. Evidence from oxygen exchange measurements for a cooperative interaction between the two heads of myosin
3. Comparative studies of oxygen exchange catalyzed by myosin, heavy meromyosin, and subfragment 1. Evidence that the γ-phosphoryl group of adenosine triphosphate binds to myosin in the region of the (subfragmental 1)-(subfragment 2) hinge
4. Oxygen exchange by single-headed myosin. Further support for the hypothesis that the active site of myosin is near the (subfragment 1)-(subfragment 2) hinge.
5. Mechanism of Hydrolysis of Adenosinetriphosphate by Muscle Proteins and Its Relation to Muscular Contraction
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1. The ATPase Reaction Cycle of Yeast DNA Topoisomerase II;Journal of Biological Chemistry;2001-07
2. Cryoenzymic studies on myosin: transient kinetic evidence for two types of head with different ATP binding properties;Biochimie;1989-03
3. Functional sequences of the myosin head;Journal of Muscle Research and Cell Motility;1989-02
4. Two pathways for oxygen exchange by heavy meromyosin and their dependence on actin.;Journal of Biological Chemistry;1988-04
5. Anomalous oxygen-18 exchange during ATP synthesis in oxidative phosphorylation;Biochemistry;1986-10-07
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