Myosin ATP Hydrolysis: A Mechanism Involving a Magnesium Chelate Complex
- 1 December 1973
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 70 (12) , 3793-3796
- https://doi.org/10.1073/pnas.70.12.3793
Abstract
It is suggested that under physiological conditions (> 1 mM Mg2+) MgATP binds to myosin to form a chelate involving the two reactive sulfhydryl sites (SH1 and SH2). The stability of the chelate structure results in marked inhibition of the myosin ATPase in the presence of millimolar magnesium ion. The inhibitory effect of magnesium ion can be eliminated chemically by blocking either the SH1 or SH2 site since this precludes formation of the chelate. In muscle, actin apparently behaves in a similar fashion in that its interaction with myosin causes a disruption of the chelate structure.Keywords
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