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PMID: 4272702 Published · ppublish English Journal Article

Myosin ATP hydrolysis: a mechanism involving a magnesium chelate complex.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 70 ·No. 12 ·1973-12-00 ·Pages 3793-6

Burke M, Reisler E, Harrington WF

Abstract

It is suggested that under physiological conditions (> 1 mM Mg(2+)) MgATP binds to myosin to form a chelate involving the two reactive sulfhydryl sites (SH(1) and SH(2)). 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 SH(1) or SH(2) 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.

MeSH Terms
Adenosine Triphosphatases/antagonists & inhibitors Adenosine Triphosphate/metabolism Binding Sites Chelating Agents Hydrogen-Ion Concentration Hydrolysis Ligands Magnesium/pharmacology Myosins/antagonists & inhibitors,metabolism Structure-Activity Relationship Sulfhydryl Compounds
Chemicals
Chelating Agents Ligands Sulfhydryl Compounds Adenosine Triphosphate Adenosine Triphosphatases Myosins Magnesium
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Burke M
Reisler E
Harrington W F
References (19)
19 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.70.12.3793
Published
1973-12-00
Pages
3793-6
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC427330
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.70.12.3793 PMC Full Text View journal details
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