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Quiz

Biol 334 continued

Margaret MacMillan 44 Fragen

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  1. 1For the reaction A -----> B, ΔGo' = -32 kJ/mol.
    The reaction is started in water (in a test-tube) with 10 mmol of A & 0 mmol B. After 48 hours, chemical analysis revealed the presence of 8 mmol A, & 2 mmol B.
    Which is the likely explanation?
    1. AA and B have attained equilibrium concentrations
    2. BEquilibrium has not been reached since B formation is kinetically slow
    3. CThe result described is impossible, given that ΔGo' = - 32 kJ/mol
    4. DAn enzyme has shifted the equilibrium to A
    5. EFormation of B is thermodynamically unfavourable
  2. 2Which of the following statements is NOT correct
    1. AIf the Keq for a chemical reaction is much smaller than its mass action ratio then the forward reaction is favored.
    2. BNear-equilibrium enzymes catalyze reversible reactions.
    3. CThe more a reaction is displaced from equilibrium, the more negative its ΔG’ becomes
    4. DFor a reaction catalyzed by a ‘non-equilibrium’ enzyme, Keq will be far larger than the mass action ratio.
    5. ENon-equilibrium enzymes control flux through metabolic pathways.
  3. 3Acetyl-CoA hydrolase catalyzes the following reaction: acetyl-CoA + H20 → acetate + CoA.
    A chemist is provided with the following information:
    Oxaloacetate + acetyl-CoA + H20 → citrate + CoA ; ΔGo' = -32 kJ/mol
    Oxaloacetate + acetate → citrate ; ΔGo' = -2 kJ/mol
    From this information the biochemist concludes that the reaction catalyzed by acetyl-CoA hydrolase:
    1. Ais at equilibrium in vivo.
    2. Bis displaced from equilibrium in vivo.
    3. Cis exothermic (or ‘exergonic’).
    4. Drequires an energy input in order to proceed in the forward (acetate producing) direction.
    5. Erequires an allosteric activator before it will occur in vivo.
  4. 4Complete the following sentence correctly. The majority of enzymes in a catabolic pathway…
    1. Acatalyze a reaction having a highly negative ΔG’
    2. Bcatalyze a reaction for which the equilibrium constant (Keq ) approximately equals the mass action ratio
    3. Cmarkedly lower the ΔGo’ for the reaction that they catalyze
    4. Dare allosteric ‘pacemaker’ enzymes
    5. Egenerate ATP via “substrate level phosphorylation”
  5. 5Under what special circumstance is the following equation the correct expression for the actual (in vivo) free-energy change of the reaction A -----> B?
    G= = Go’ + RTlnKeq
    1. AWhen the reaction is highly exothermic.
    2. BWhen the activation energy has been lowered
    3. CWhen the enthalpy of the reaction has been exceeded
    4. DWhen the reaction is greatly displaced from equilibrium in vivo
    5. EWhen the reaction is at equilibrium in vivo.
  6. 6The hydrolytic reaction: ATP + H20  ADP + Pi, has a standard free energy change, ΔGo’ = -30.5 kJ/mol
    The actual (in vivo) free energy change for this reaction in healthy red blood cells = ΔG’ = -50 kJ/mol
    What do these ΔGo’ &/or ΔG’ values tell us about ATP hydrolysis (to ADP + Pi)?
    1. Athe reaction is close to equilibrium in the red blood cell
    2. Bthe equilibrium position for this reaction greatly favours the products, ADP + Pi
    3. Cthis reaction is greatly displaced from equilibrium in the red blood cell
    4. DA & B are both correct
    5. EB & C are both correct
  7. 7A new species of bacteria, Comparata biochemica, was discovered that catalyzes the following reaction:
    Lactate  Ethanol + CO2
    Calculate the standard free energy change (ΔGo') for the above reaction, from the following information:
    acetaldehyde + CO2 → pyruvate ΔGo’ = +19.8 kJ/mol
    acetaldehyde + NADH + H+ → ethanol + NAD+ ΔGo’ = -23.7 kJ/mol
    pyruvate + NADH + H+ → lactate + NAD+ ΔGo’ = -25.1 kJ/mol
    1. A+18.4 kJ/mol
    2. B-48.8 kJ/mol
    3. C-18.4 kJ/mol
    4. D-68.6 kJ/mol
    5. E+3.9 kJ/mol
  8. 8The ΔGo' values for the 3 different reactions shown below are given:
    1. Malate + NAD+ -----------> Oxaloacetate + NADH + H+ ΔG o' = +30 kJ/mol
    2. Oxaloacetate + acetyl-CoA + H2O --------> Citrate + CoA ΔG o' = -32 kJ/mol
    3. Oxaloacetate + acetate -----------> Citrate ΔG o'= -2 kJ/mol
    What is the ΔG o' value for acetyl-CoA hydrolysis?
    i.e., Acetyl-CoA + H2O ----> Acetate + CoA , ΔG o' = ???
    1. A+30 kJ/mol
    2. B-34 kJ/mol
    3. C-62 kJ/mol
    4. D-30 kJ/mol
    5. ECan’t compute from information given
  9. 9The bacteria Pseudomonas. saccharophila contains sucrose phosphorylase, an enzyme that catalyzes the phosphorolytic cleavage of sucrose as follows: Sucrose + Pi -----------> Glucose-1-P + Fructose.
    Calculate the standard free energy change (ΔGo') for the above reaction, from the following data.
    1. H2O + Sucrose --------> Glucose + Fructose; ΔG o' = -7.0 kcal/mol
    2. H2O + Glucose-1-phosphate --------> Glucose + Pi; ΔG o' = -5.0 kcal/mol.
    1. A-12 kcal/mol
    2. B-2.0 kcal/mol
    3. C+2.0 kcal/mol
    4. D+12 kcal/mol
    5. Ecannot compute without additional information
  10. 10Which of the following statements concerning the "control analysis" approach to metabolic control is FALSE?
    1. Aa flux control coefficient of 0.8 suggests that this particular enzyme is relatively unimportant in controlling pathway flux
    2. Bits application does not require prior knowledge of which enzyme(s) in the pathway catalyze the "pacemaker" or "rate determining step" of the entire pathway.
    3. Cit predicts that pathway control is shared (to varying degrees) by all the enzymes of the pathway.
    4. Dit provides a way to quantify the relative contribution of each enzyme in a pathway to overall regulation of pathway flux in the intact system.
    5. Eit is based upon the fact that biological systems may display regulatory properties not possessed by the isolated components.

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Beschreibung
Biology Quiz am Biol 334 continued, erstellt von Margaret MacMillan am 10/02/2019.
Sprache
English
Aufrufe
6
Schlagwörter
biology
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