Myosin ATP Hydrolysis: A Mechanism Involving a Magnesium Chelate Complex
AUTOR(ES)
Burke, Morris
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=427330Documentos Relacionados
- Assembly of a functional replication complex without ATP hydrolysis: a direct interaction of bacteriophage T4 gp45 with T4 DNA polymerase.
- Regulation of actin-activated ATP hydrolysis by arterial myosin.
- Osmotic pressure probe of actin-myosin hydration changes during ATP hydrolysis.
- Measuring Endocannabinoid Hydrolysis: Refining our Tools and Understanding
- Coupling of protein surface hydrophobicity change to ATP hydrolysis by myosin motor domain.
