For a unimoleclar irreversible reaction, A -----> B, once the reactant A has entirely been converted to product B, the end of the reaction is given by   Question 12 options:   k[B]   d[A]/dT = -d[B]/dT   dB/dT = -dA/dT   dB/dT = 0

Which of the following statements are true for BOTH the "transition state" and an "intermediate" of reaction? (This is a multi-select question, select all that apply.). Both are only observed in enzyme-catalyzed reactions. Both can be converted to product(s) or might decompose back to the reactant(s). Neither are part of the "net equation" for the reaction. Both contain covalent bonds are in the process of breaking and/or forming. Both are part of every chemical reaction. (i.e. the mechanisms of all chemical reactions, whether enzyme catalyzed or not, will have involve both a transition state and an intermediate).

A particular reaction has a ΔG‡ of 37.0 kJ mol-1. In the presence of an enzyme, the same reaction has a ΔG‡ of 5.70 kJ mol-1. Calculate the value of ΔΔG‡ in kJ mol-1.

The decomposition reaction of hydrogen peroxide (H₂O₂) proceeds as follows: 2 H₂0₂ → 2 H₂O + 0₂ 2 This reaction can occur without a catalyst, in the presence of a chemical catalyst (platinum) or of a biological catalyst (catalase). 1- From the values given in the table below, determine the catalytic power of each catalyst (ratio of the catalyzed rate of reaction to the uncatalyzed rate). 2- Which catalyst is the most efficient? Reaction conditions No catalyst Platinum Catalase Ea (kJ.mol¹) at 20 °C 75 49 8

Which of the following relationships is (are) correct? (Select all that apply.) DG is equal to -TDSuniv DG > 0 represents a spontaneous process in the reverse direction. None of these DG < O represents a spontaneous process in the forward direction. DG < 0 indicates the reaction will reach equilibrium quickly.

Compounds I, II, and III are in the following biochemical pathway: precursor compound I enzyme A enzyme B compound II ► compound III enzyme Mutation a inactivates enzyme A, mutation b inactivates enzyme B, and mutation c inactivates enzyme C. Mutants, each having one of these defects, were tested on minimal medium to which compound I, II, or III was added. Fill in the results expected of these tests by placing a plus sign (+) for growth or a minus sign (-) for no growth in the table below. Minimal medium to which is added Strain with mutation Compound I Compound II Compound III

An enzyme has a single active site at which it can bind and hydrolyze either X or Y; however, the enzyme cannot bind X and Y at the same time. Answer the following questions regarding the Km and Vmax of this enzyme. (a) Will the Km for X be affected if Y is present in the reaction mixture? Explain. (b) Will Vmax for X be affected if Y is present in the reaction mixture? Explain. (a) No, X competes with Y for binding, so the apparent Km for X will stay the same. (b) Yes, the Vmax for X will decrease in the presence of Y. (a) No, Y does not compete with X for binding, so the apparent Km for X will stay the same. (b) No, the Vmax for X will be unaffected by the presence of Y.

Which one of the following statements is completely TRUE? O When AG > 0, the reaction is BOTH product-favored (spontaneous) AND endergonic. When AG 0, the reaction is BOTH reactant-favored (nonspontaneous) AND endergonic. When AG > 0, the reaction is BOTH product-favored (spontaneous) AND exergonic. When AG > 0, the reaction is BOTH reactant-favored (nonspontaneous) AND exergonic. When AG < 0, the reaction is BOTH reactant-favored (nonspontaneous) AND exergonic.

When calculating the order of a reaction, the enzyme doesnot appear in the equation. Explain.

What are the benefits of measuring the initial rate of a reaction Vå for use in kinetic studies? (This is a multi-select question). [ES] can be measured accurately. changes in [S] are negligible, so the value of [S] is known. changes in Km are negligible, so Km can be treated as a constant. V₁ = Vmax. --> A negligible amount of product has formed, so that the back reaction P -- need not be considered. ES