期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1973
卷号：70
期号：12
页码：3793-3796
DOI：10.1073/pnas.70.12.3793
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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.
