Time [Z] (hours) (mg/L) 160 2 140 3 130 6 100 80 10 60 12 40 Calculate k, the elimination rate constant, responsible for drug degradation (in mg/L*hr).

In a study of the rearrangement of ammonium cyanate to urea in aqueous solution at 50 °C NHẠNCO(aq)→(NH2)½CO(aq) the concentration of NH,NCO was followed as a function of time. It was found that a graph of 1/[NH4NCO] versus time in minutes gave a straight line with a slope of 1.44×102 Ml min-1 and a y-intercept of 0.980 M-!. Based on this plot, the reaction is order in NH4NCO and the rate constant for the reaction is M1 min-1.

At pH = 7, the measured Michaelis constant and maximum velocity for the enzymatic conversion of fumarate to L-malate,   Fumarate + H2O → L-Malate   are 4.0 x 10-6 M and 1.3 x 10 3 [E]0 s-1 , respectively, where [E]0 is the total molar concentration of the enzyme.   The Michaelis constant and maximum velocity for the reverse reaction are 1.0 x 10-5 M and 800 [E]0 s-1 , respectively.   8A)WHAT is the equilibrium constant (a value) for the hydration reaction? [Notes: the arrow above is an equilibrium arrow. The activity of water is set equal to unity]   8B.) DRAW all chemical entities in the forward, balanced chemical reaction, above.

In a study of the gas phase decomposition of sulfuryl chloride at 600 KSO2Cl2(g)SO2(g) + Cl2(g)the concentration of SO2Cl2 was followed as a function of time.It was found that a graph of ln[SO2Cl2] versus time in minutes gave a straight line with a slope of -4.28×10-3 min-1 and a y-intercept of -6.95 . Based on this plot, the reaction is________. (firest, zero, or second) order in SO2Cl2 and the rate constant for the reaction is min-1.

The protein catalase catalyzes the reaction 2H,0,(aq) – 2 H,0O(0) + 0,(g) and has a Michaelis–Menten constant of KM = 25 mM and a turnover number of 4.0 × 107 s-1. The total enzyme concentration is 0.016 µM and the initial substrate concentration is 6.58 µM. Catalase has a single active site. Calculate the value of Rmax (often written as Vmax ) for this enzyme. Rmax mM-s- Calculate the initial rate, R (often written as Vo), of this reaction. R = mM-s-

Suppose that a certain biologically important reaction is quite slow at physiological temperature (37 °C) in the absence of a catalyst Part A Assuming that the collision factor remains the same, by how much must an enzyme lower the activation energy of the reaction in order to achieve a 5x105-fold increase in the reaction rate? Express your answer in kilojoules per mole to one significant figure. ΠΕΙ ΑΣΦ Ea,uncatalyzed - Ea,catalyzed 148 Sulmit Previous Answers Request Answer M Incorrect: Try Again: One attempt remaining Review Constants | Periodic Table ? kJ/mol

1-arr In a study of the decomposition of dinitrogen pentoxide in carbon tetrachloride solution at 30 °C N2O5- →2 NO2 + ½ O2 the concentration of N,O5 was followed as a function of time. It was found that a graph of In[N2O5] versus time in minutes gave a straight line with a slope of -6.31×10* min and a y- intercept of -1.34 . Based on this plot, the reaction O order in N,0g and the rate constant for the reaction is min-1. zero first second

[RCOOH], M [R’OH], M [HA], M Initial Rate, M-min 23. 0.35 0.35 0.50 4.60 0.62 0.35 0.50 8.14 0.35 0.81 0.50 10.6 0.35 0.50 0.75 9.84 Rate = k[RCOOH][R'OH] Rate = k[RCOOH][R'OH][HA] Rate = k[RCOOR']/{[RCOOH][R'OH]} Rate = k[R'OH] Rate = k[RCOOH] 26. The initial reaction rate for the reaction in question 23 can be followed spectrophotometrically by quenching the reaction and determining the amount of R'OH left by its reaction with the dichromate ion, Cr20-2-. Write a balanced equation for the reaction of Cr20,2- with R'OH in acid solution. For simplicity, you may assume R' is an ethyl group (CH3CH2) and the products of the reaction are Cr3+ and CH3COOH. ЗСНЗСН20Н() + 2Cr2072-(аq) + 16H+{аq) + 3СНЗСООН() 4C13+(aq) + 3CH3COOCH3(I) + 14H2O(1) --> 3CH3CH2OH(I) + 2Cr2072-(aq) + 16H+(aq) ЗСНЗСООН() + 11Н20() 4Cr3+(aq)+ + --> --> 4CR3+(aq)++ 3CH3CH2OH(I) + 2Cr2072-(aq) + 5H2O(I) ЗСНЗСООН() + 160H-(аq) CH3CH2OH(I) + Cr2072-(aq) 2Cr3+(aq)+ + CH3COOH(I) --> СНЗCН2ОH() + Cr2072-(aq) Cr3+(aq)+ +…

A protein catalyzes the following reaction and had a Michaelis-Menten constant of  Km=25 mM and a turnover number of 4.0 x 107 s-1. The total enzyme concentration is 0.012 µM and the initial substrate concentration is 4.76 µM. The enzyme has a single active site. Calculate the values of Vmax and V0  for this enzyme. 2H2O2 (aq) -----> 2H2O(l) + O2(g) Vmax= Vo=

Temperature effect on the degradation of a multisulfa preparation was evaluated at 60 and 70°C. If the first-order reaction rate constants responsible for the degradation at these two temperatures were 8.2 x 10-4 and 1.96 x 10-3 hr-1, respectively, answer the following TWO questions.   Calculate the frequency factor, A, for the degradation of this drug within this temperature range (in hr-1).