What would be the standard free energy change if FADH 2 is used to reduce O 2 to water? Standard reduction potential values to be used for calculations.
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- What would be the standard free energy change if FADH 2 is used to reduce O 2 to water? Standard reduction potential values to be used for calculations. BIU (.a >5 €. Σ FMThe energy of activation for the reaction 2 HI – H2 + I2 is 180. kJ•mol-1 at 544 K. Calculate the rate constant using the equation k = Ae-EalRT. The collision diameter for HI is 3.5×10-8 cm. Assume that the pressure is 1.00 atm. 4.0 4.510e-27 X M-1.s-1For the following results of Thermodynamics of Borax Solubility, the volume of Borax solution titrated by HCI is 8.00 mL. Table 1. Volumes of hydrochloric acid required to titrate a saturated borax solution at varying temperatures. The hydrochloric acid was a solution standardized at 0.2912 M. Borax Volume added (mL) Temp. (°C) 8.00 8.00 8.00 8.00 8.00 HCI Volume (mL) 50.5 33.75 40.7 27.02 30.0 17.95 20.2 13.43 10.3 8.55 Using Thermodynamic formula (R= 8.31 J/K⚫mol) and the above results, (b) What is the y-intercept of the best fitting line for this data? Type your answer...
- For the following results of Thermodynamics of Borax Solubility, the volume of Borax solution titrated by HCI is 8.00 mL. Table 1. Volumes of hydrochloric acid required to titrate a saturated borax solution at varying temperatures. The hydrochloric acid was a solution standardized at 0.2912 M. Borax Volume added (mL) Temp. (°C) 8.00 8.00 8.00 8.00 8.00 HCI Volume (mL) 50.5 33.75 40.7 27.02 30.0 17.95 20.2 13.43 10.3 8.55 Using Thermodynamic formula (R= 8.31 J/K•mol) and the above results, (e) AS° = (J/K⚫mol) Type your answer...Calculate the Keq (report up to two decimal places and do not use scientific notation) for the net reaction at 298.15K. (see attached image) Note: R = 1.98 x 10 -3 kcal/mol-KFrom your Lineweaver-Burk plot,the vlaues are: Km Vmax Uninhibited 0.09 mmol/L 3.02 min/mmol Inhibited 6.22 mmol/L 9.98 min/mmol By describing the potential changes in the kinetic parameters, identify and justify the type of inhibitor that was inhibiting the acid phosphatase activity.
- Suppose that the data shown in the margin are obtained for an enzyme -catalyzed reaction. [S] (mM) V (mmol/ml min) 0.1 3.33 0.2 5.0 0.5 7.14 0.8 8.00 1.0 8.33 2.0 9.09 a.) Determine the Km and Vmaxb.) Assuming htat the enzyme present in the system had a concentration of 10-6M, calculate the turn -over numberThe following results were obtained for an enzyme-catalysed reaction Substrate concentration (mmol r'): 5.0 Initial velocity (umol l' min'): 6.67 10.0 20.0 40.0 147 182 233 323 400 Calculate Km and VmaxAn enzyme catalyzes a reaction with a Km of 9.50 mM and a Vmax of 2.10 mM · s-1. Calculate the reaction velocity, vo, for each substrate concentration. [S] = 3.25 mM vo : mM · s-1 [S] = 9.50 mM mM · s-1 Vo :
- Given the following set of kinetic data, what is the KM of the enzyme? Numerical answer, only (assuming the same units as seen in the table). [S] (micro M) vo (Micro mol/sec) 1 49 2 96 8 249 50 498 100 656 1000 778 5000 999Calculate AG for the below balanced redox reaction as written. You may find a list of standard reduction potentials useful. 3 12 (s) + 2 Al (s) → 61 (aq) + 2 Al3+ (aq) O-4.24 x 102 kJ/mol O-6.48 x 102 kJ/mol O -2.12 x 102 kJ/mol O-1.27 x 103 kJ/mol O-6.37 x 102 kJ/molThe maximum saturation, 28.3ug of enzyme in 25ml water catalyzes the oxidation of ethanol at a rate of 2.5mm/min. Calculate the kcat in units of seconds if the enzyme has a molar mass of 65kg/mol.