Literature DB >> 2829836

A transient kinetic study of enthalpy changes during the reaction of myosin subfragment 1 with ATP.

N C Millar1, J V Howarth, H Gutfreund.   

Abstract

1. The enthalpy changes during individual reaction steps of the myosin subfragment 1 ATPase were studied with the use of a new stopped-flow calorimeter [Howarth, Millar & Gutfreund (1987) Biochem. J. 248, 677-682]. 2. At 5 degrees C and pH 7.0, the endothermic on-enzyme ATP-cleavage step was observed directly (delta H = +64 kJ.mol-1). 3. ADP binding is accompanied by a biphasic enthalpy change. 4. The release and uptake of protons was investigated by the use of two buffers with widely different heats of ionization. 5. Protons are involved in all four principal steps of the myosin subfragment 1 ATPase.

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Year:  1987        PMID： 2829836      PMCID： PMC1148603          DOI： 10.1042/bj2480683

Source DB:  PubMed          Journal:  Biochem J        ISSN： 0264-6021            Impact factor:   3.857


  25 in total

1.  Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin.

Authors:  A G Weeds; R S Taylor
Journal:  Nature       Date:  1975-09-04       Impact factor: 49.962

2.  Intermediate states of actomyosin adenosine triphosphatase.

Authors:  J A Sleep; E W Taylor
Journal:  Biochemistry       Date:  1976-12-28       Impact factor: 3.162

3.  The enthalpy change of adenosine triphosphate hydrolysis.

Authors:  R J PODOLSKY; M F MORALES
Journal:  J Biol Chem       Date:  1956-02       Impact factor: 5.157

Review 4.  Kinetic analysis of ATPase mechanisms.

Authors:  D R Trentham; J F Eccleston; C R Bagshaw
Journal:  Q Rev Biophys       Date:  1976-05       Impact factor: 5.318

5.  Heavy meromyosin Mg-ATPase: presteady-state and steady-state Hplus release.

Authors:  S P Chock; E Eisenberg
Journal:  Proc Natl Acad Sci U S A       Date:  1974-12       Impact factor: 11.205

6.  Effect of pH and metal ion concentration on the equilibrium hydrolysis of adenosine triphosphate to adenosine diphosphate.

Authors:  R A Alberty
Journal:  J Biol Chem       Date:  1968-04-10       Impact factor: 5.157

7.  Transient state kinetic studies of proton liberation by myosin and subfragment 1.

Authors:  J F Koretz; E W Taylor
Journal:  J Biol Chem       Date:  1975-08-25       Impact factor: 5.157

8.  The characterization of myosin-product complexes and of product-release steps during the magnesium ion-dependent adenosine triphosphatase reaction.

Authors:  C R Bagshaw; D R Trentham
Journal:  Biochem J       Date:  1974-08       Impact factor: 3.857

9.  Transient phase of adenosine triphosphate hydrolysis by myosin, heavy meromyosin, and subfragment 1.

Authors:  E W Taylor
Journal:  Biochemistry       Date:  1977-02-22       Impact factor: 3.162

10.  Calorimetric studies of the interaction of myosin with ADP.

Authors:  T Kodama; R C Woledge
Journal:  J Biol Chem       Date:  1976-12-10       Impact factor: 5.157
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  9 in total

Review 1.  The structural basis of muscle contraction.

Authors:  K C Holmes; M A Geeves
Journal:  Philos Trans R Soc Lond B Biol Sci       Date:  2000-04-29       Impact factor: 6.237

Review 2.  Force and power generating mechanism(s) in active muscle as revealed from temperature perturbation studies.

Authors:  K W Ranatunga
Journal:  J Physiol       Date:  2010-10-01       Impact factor: 5.182

3.  A transient-kinetic study of the nitrogenase of Klebsiella pneumoniae by stopped-flow calorimetry. Comparison with the myosin ATPase.

Authors:  R N Thorneley; G Ashby; J V Howarth; N C Millar; H Gutfreund
Journal:  Biochem J       Date:  1989-12-15       Impact factor: 3.857

4.  A stopped-flow calorimeter for biochemical applications.

Authors:  J V Howarth; N C Millar; H Gutfreund
Journal:  Biochem J       Date:  1987-12-15       Impact factor: 3.857

5.  Temperature dependence of active tension in mammalian (rabbit psoas) muscle fibres: effect of inorganic phosphate.

Authors:  M E Coupland; E Puchert; K W Ranatunga
Journal:  J Physiol       Date:  2001-11-01       Impact factor: 5.182

6.  Endothermic force generation, temperature-jump experiments and effects of increased [MgADP] in rabbit psoas muscle fibres.

Authors:  M E Coupland; G J Pinniger; K W Ranatunga
Journal:  J Physiol       Date:  2005-06-23       Impact factor: 5.182

7.  An analysis of the temperature dependence of force, during steady shortening at different velocities, in (mammalian) fast muscle fibres.

Authors:  H Roots; K W Ranatunga
Journal:  J Muscle Res Cell Motil       Date:  2008-06-04       Impact factor: 2.698

8.  Nitrogenase of Klebsiella pneumoniae. Reversibility of the reductant-independent MgATP-cleavage reaction is shown by MgADP-catalysed phosphate/water oxygen exchange.

Authors:  R N Thorneley; G A Ashby; C Julius; J L Hunter; M R Webb
Journal:  Biochem J       Date:  1991-08-01       Impact factor: 3.857

Review 9.  Temperature Effects on Force and Actin⁻Myosin Interaction in Muscle: A Look Back on Some Experimental Findings.

Authors:  K W Ranatunga
Journal:  Int J Mol Sci       Date:  2018-05-22       Impact factor: 5.923
  9 in total

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