Two pathways for oxygen exchange by heavy meromyosin and their dependence on actin.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference27 articles.
1. 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.
2. The equivalence of phosphate oxygens for exchange and the hydrolysis characteristics revealed by the distribution of [18O]Pi species formed by myosin and actomyosin ATPase.
3. 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.
4. On the mechanism of actomyosin ATPase from fast muscle.
5. Oxygen-exchange studies on the pathways for magnesium adenosine 5'-triphosphate hydrolysis by actomyosin
Cited by 5 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Skeletal muscle myosin subfragment 1 dimers;Biophysical Chemistry;1997-03
2. Half-stoichiometric trinitrophenylation of myosin subfragment 1 in the presence of pyrophosphate or adenosine diphosphate.;Journal of Biological Chemistry;1993-04
3. Kinetics of ATP and inorganic phosphate release during hydrolysis of ATP by rabbit skeletal actomyosin subfragment 1. Oxygen exchange between water and ATP or phosphate.;Journal of Biological Chemistry;1990-01
4. Intermediate oxygen exchange catalyzed by the actin-activated skeletal myosin adenosine triphosphatase;Biochemistry;1989-09-19
5. Measurement of the reversibility of ATP binding to myosin in calcium-activated skinned fibers from rabbit skeletal muscle;Journal of Biological Chemistry;1989-05
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