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.
Open Access
- 1 December 1978
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 253 (23) , 8362-8365
- https://doi.org/10.1016/s0021-9258(17)34299-0
Abstract
No abstract availableThis publication has 13 references indexed in Scilit:
- 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) hingeBiochemistry, 1977
- Mechanism of oxygen exchange in actin-activated hydrolysis of adenosine triphosphate by myosin subfragment 1Biochemistry, 1977
- The location of the divalent metal binding sites and the light chain subunits of vertebrate myosinBiochemistry, 1977
- Effect of DTNB light chain on the interaction of vertebrate skeletal myosin with actinNature, 1975
- Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosinNature, 1975
- Interaction of actin with N-ethylmaleimide modified heavy meromyosin in the presence and absence of adenosine triphosphateBiochemistry, 1975
- Oxygen exchange in the gamma-phosphoryl group of protein-bound ATP during Mg2+-dependent adenosine triphosphatase activity of myosin.Proceedings of the National Academy of Sciences, 1975
- The reversibility of adenosine triphosphate cleavage by myosinBiochemical Journal, 1973
- Mechanism of adenosine triphosphate hydrolysis by actomyosinBiochemistry, 1971
- Mechanism of Hydrolysis of Adenosinetriphosphate by Muscle Proteins and Its Relation to Muscular ContractionJournal of Biological Chemistry, 1959