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. 1973 Dec;70(12 Pt 1-2):3793–3796. doi: 10.1073/pnas.70.12.3793

Myosin ATP Hydrolysis: A Mechanism Involving a Magnesium Chelate Complex

Morris Burke 1, Emil Reisler 1, William F Harrington 1
PMCID: PMC427330  PMID: 4272702

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: muscle, sulfhydryl sites, ATPase, actin

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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