ArticleBiophysical journal1994
Kinetic mechanism of myofibril ATPase.
Article in Biophysical journal, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 82 citations in OpenAlex.
- Actin-binding compounds, previously discovered by FRET-based high-throughput screening, differentially affect skeletal and cardiac muscle.The Journal of biological chemistry · 2020Article
- Effect of N-Terminal Extension of Cardiac Troponin I on the Ca(2+) Regulation of ATP Binding and ADP Dissociation of Myosin II in Native Cardiac Myofibrils.Biochemistry · 2016Article
- Poorly understood aspects of striated muscle contraction.BioMed research international · 2015Review
- A new mechanokinetic model for muscle contraction, where force and movement are triggered by phosphate release.Journal of muscle research and cell motility · 2014Article
- Velocity-dependent actomyosin ATPase cycle revealed by in vitro motility assay with kinetic analysis.Biophysical journal · 2012Article
- Correlation between cross-bridge kinetics obtained from Trp fluorescence of myofibril suspensions and mechanical studies of single muscle fibers in rabbit psoas.Journal of muscle research and cell motility · 2011Article
- Drug effect unveils inter-head cooperativity and strain-dependent ADP release in fast skeletal actomyosin.The Journal of biological chemistry · 2009Article
- Insights into the kinetics of Ca2+-regulated contraction and relaxation from myofibril studies.Pflugers Archiv : European journal of physiology · 2009Article
- Effect of inorganic phosphate on the force and number of myosin cross-bridges during the isometric contraction of permeabilized muscle fibers from rabbit psoas.Biophysical journal · 2008Article
- Kinetic mechanism of the Ca2+-dependent switch-on and switch-off of cardiac troponin in myofibrils.Biophysical journal · 2007Article
- Kinetics of muscle contraction and actomyosin NTP hydrolysis from rabbit using a series of metal-nucleotide substrates.The Journal of physiology · 2005Article
- The ATP hydrolysis and phosphate release steps control the time course of force development in rabbit skeletal muscle.The Journal of physiology · 2005Article
- Structural transients of contractile proteins upon sudden ATP liberation in skeletal muscle fibers.Biophysical journal · 2004Article
- Inorganic phosphate affects the pCa-force relationship more than the pCa-ATPase by increasing the rate of dissociation of force generating cross-bridges in skinned fibers from both EDL and soleus muscles of the rat.Journal of muscle research and cell motility · 2004Article
- Why choose myofibrils to study muscle myosin ATPase?Journal of muscle research and cell motility · 2003Review
- Myosin V exhibits a high duty cycle and large unitary displacement.The Journal of cell biology · 2001Article
- Is SH1-SH2-cross-linked myosin subfragment 1 a structural analog of the weakly-bound state of myosin?Biophysical journal · 2000Article
- A thermodynamic muscle model and a chemical basis for A.V. Hill's muscle equation.Journal of muscle research and cell motility · 2000Article
- Regulation of force and unloaded sliding speed in single thin filaments: effects of regulatory proteins and calcium.The Journal of physiology · 2000Article
- Cross-bridge attachment during high-speed active shortening of skinned fibers of the rabbit psoas muscle: implications for cross-bridge action during maximum velocity of filament sliding.Biophysical journal · 2000Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The kinetic mechanism of myofibril ATPase was investigated using psoas and mixed back muscle over a range of ionic strengths. Myofibrils were labeled with pyrene iodoacetamide to measure the rate constants for the binding of ATP and formation of the weakly attached state. The velocity of shortening was measured by stopping the contraction at various times by mixing with pH 4.5 buffer. The transient and steady-state rates of ATP hydrolysis were measured by the quench flow method. The results fitted the kinetic scheme [formula: see text] The rate constants (or equilibrium constants for steps 1 and 6) were obtained for the six steps. k5 was calculated from the KM for shortening velocity, K1, and k2. The rate constants were essentially equal for myofibrils and acto-S-1 at low ionic strength. Increasing the ionic strength up to 100 mM in NaCl increased the rate of the hydrolysis step and the size of the phosphate burst and the effective rate of product release became the rate-limiting step. The step calculated from the velocity of shortening, k5, and k2 is 15 nm, based on a model in which step 4 is the force-generating step.
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