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Related Experiment Videos

Probing actomyosin interactions with 2,4-dinitrophenol.

A S Ribeiro1, V P Salerno, M Sorenson

  • 1Instituto de Bioquímica Médica, Universidade Federal do Rio de Janeiro, Rio de Janeiro, 21941-590 RJ, Brazil.

Biochimica Et Biophysica Acta
|March 17, 2005
PubMed
Summary

2,4-Dinitrophenol (DNP) impacts muscle contraction by increasing the affinity of actin to myosin while slowing turnover. This leads to stabilized weakly bound cross-bridges, reducing muscle force.

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Area of Science:

  • Muscle physiology
  • Biochemistry
  • Molecular motors

Background:

  • Understanding chemomechanical coupling in muscle contraction requires studying intermediates post-ATP cleavage.
  • 2,4-Dinitrophenol (DNP) accelerates isolated myosin ATPase activity but inhibits muscle contraction.

Purpose of the Study:

  • Investigate the action of DNP on myosin subfragment 1 (S1), acto-S1, and skinned fibers in the presence of actin.
  • Elucidate the mechanism by which DNP affects muscle contraction and cross-bridge dynamics.

Main Methods:

  • Utilized myosin subfragment 1 (S1), acto-S1, and mammalian skinned fibers.
  • Measured acto-S1 affinity and turnover rates in the presence of DNP.
  • Analyzed isometric force reduction and Pi release kinetics.

Related Experiment Videos

  • Performed Arrhenius plot analysis and studied the effect of Pi concentration on force.

    • Main Results:

    • DNP increased acto-S1 affinity and reduced maximum turnover rate.
    • Isometric force in skinned fibers was reduced by DNP.
    • DNP reduced the ratio of actin-activated Pi release to acto-S1 turnover by 30-fold.
    • DNP and meta-nitrophenol (MNP) stabilize weakly bound cross-bridges (AM.ADP.Pi).
    • MNP increased apparent affinity for Pi.

    Conclusions:

    • DNP's inhibition of muscle contraction stems from a combination of enhanced S1 activity and reduced acto-S1 activity.
    • DNP and MNP likely stabilize the weakly bound AM.ADP.Pi state, impacting the muscle contraction cycle.
    • The findings provide insight into chemomechanical coupling mechanisms in skeletal muscle.