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Hydrolysis Gibbs energy changes

Figure 10.1 Standard transformed Gibbs energies of hydrolysis of phosphate compounds and changes in the binding of hydrogen ions as a function of pH at 298.15 K and 0.25 M ionic strength. Figure 10.1 Standard transformed Gibbs energies of hydrolysis of phosphate compounds and changes in the binding of hydrogen ions as a function of pH at 298.15 K and 0.25 M ionic strength.
A fast micromcthod (10-15 nmol scale) for the identification of glycosyl phosphate anomers based on spectrophotometric measurement of the rate of dieir acid-catalysed hydrolysis has been described. The standard Gibbs free-energy change for hydrolysis of a-D-ribose 1-phosphate has been determined. [Pg.54]

The standard Gibbs energy, enthalpy, and entropy changes for the hydrolysis of adeno ine-5 triphosphate to adenosine-5 -diphosphate are computed as a function of pH and aiagnesium ion concentration at 25 °C. A critical evaluation of the relevant literature data is included. Also see item [120]... [Pg.743]

The efficiency of the proton pump is defined as the total chemical and electrical work produced in unit time divided by the power made available from the hydrolysis of ATP, that is the Gibbs free energy change of hydrolysis in unit time... [Pg.173]

See other pages where Hydrolysis Gibbs energy changes is mentioned: [Pg.141]    [Pg.296]    [Pg.296]    [Pg.296]    [Pg.410]    [Pg.977]    [Pg.1700]    [Pg.3]    [Pg.296]    [Pg.296]    [Pg.296]    [Pg.410]    [Pg.64]    [Pg.787]    [Pg.43]    [Pg.766]    [Pg.383]    [Pg.771]    [Pg.789]    [Pg.347]    [Pg.422]    [Pg.136]    [Pg.302]    [Pg.1108]    [Pg.366]    [Pg.73]    [Pg.76]    [Pg.291]    [Pg.130]    [Pg.462]    [Pg.302]    [Pg.1290]    [Pg.195]    [Pg.195]    [Pg.985]    [Pg.174]    [Pg.174]    [Pg.130]    [Pg.62]    [Pg.792]    [Pg.83]    [Pg.173]    [Pg.173]    [Pg.47]    [Pg.92]    [Pg.27]   
See also in sourсe #XX -- [ Pg.2 ]



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