BIOLOGY
5th Edition
ISBN: 9781265202859
Author: BROOKER
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Chapter 6, Problem 1CQ
Summary Introduction
To determine: The differences between endergonic and exergonic reactions with regard to the rate and direction of reactions.
Introduction: In a
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The following questions are based on the reaction A+ B ↔ C+D shown in Figure 8.1.
1. Which of the following terms best describes the progress of the reaction with respect to free energy change?
a) endergonic, ∆G> 0
b) exergonic, ∆G> 0
c) exergonic, ∆G< 0
d) endergonic, ∆G< 0
2. Which of the following in Figure 8.1 remains unchanged by having an enzyme included?
a) b
b) d
c) a
d) c
3. The part labeled “C” on the above graph represents
a) Energy of activation without enzyme
b) Energy of activation with enzyme
c) Amount of free energy released
d) amount of energy required for the reaction progress
Derive the complete rate equation using the King altman method. Example is shown above the reaction mechanism. All the N terms must be derived.
What do the following indicators tell you about whether a reaction can proceed as written? (a) The standard free-energy change is positive. (b) The free-energy change is positive. (c) The reaction is exergonic
Chapter 6 Solutions
BIOLOGY
Ch. 6.1 - Which do you think has more entropy, a NaCl...Ch. 6.1 - Prob. 2CCCh. 6.2 - Prob. 1CCCh. 6.2 - Prob. 2CCCh. 6.2 - Prob. 1CSCh. 6.2 - Prob. 1EQCh. 6.2 - Prob. 2EQCh. 6.2 - Prob. 3EQCh. 6.3 - Prob. 1CSCh. 6.3 - Prob. 2CS
Ch. 6.4 - What are advantages of protein degradation?Ch. 6 - Reactions that release free energy are a....Ch. 6 - Enzymes speed up reactions by a. providing...Ch. 6 - Prob. 3TYCh. 6 - Researchers analyzed a cell extracta mixture of...Ch. 6 - In biological systems, ATP functions by a....Ch. 6 - In a chemical reaction, NADH is converted to NAD+...Ch. 6 - Prob. 7TYCh. 6 - Prob. 8TYCh. 6 - Prob. 9TYCh. 6 - Autophagy provides a way for cells to a. degrade...Ch. 6 - Prob. 1CQCh. 6 - Prob. 2CQCh. 6 - Prob. 3CQCh. 6 - Prob. 1COQCh. 6 - Prob. 2COQ
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- discuss the following statement: “Whether the ΔG for a reaction is larger, smaller, or the same as ΔG° depends on the concentration of the compounds that participate in the reaction.”arrow_forwardFor the reversible, liquid-phase reaction A ↔ B, determine the adiabatic equilibrium temperature and conversion when pure A is fed to the reactor at 300 K. CPA = CPB = 50 cal mol¹ K-¹. Heat capacities are independent of temperature. The equilibrium constant is 1.0 × 105 at 298 K; the heat of reaction is -2.0 × 10 cal/mol.arrow_forwardFor a particular reaction, AH° = −16.1 kJ/mol and AS° = −21.8 J/(mol·K). Assuming these values change very little with temperature, at what temperature does the reaction change from nonspontaneous to spontaneous in the forward direction? OT= Is the reaction in the forward direction spontaneous at temperatures greater than or less than the calculated temperature? less than greater than Karrow_forward
- 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).arrow_forwardDetermine whether or not reaction is a redox reaction. For each redox reaction, identify the oxidizing agent and the reducing agent. HBr(aq) + KOH(aq)--------> H2O(l) + KBr(aq)arrow_forwardConsider the reaction below to answer the following question(s): + HBr A B Br с + D Br Enter the appropriate letter in the blank for each the following statements. The kinetically controlled product in this reaction is D B Aarrow_forward
- Enzymes are biological catalysts that fulfill the following general reaction mechanism: E+S [ES] [EP] E + P Where E is enzyme, S is substrate, and P is product. Briefly describe how an enzyme is able to speed of the rate of a reaction:arrow_forwardShow that the half-life for a first-order reaction is inversely proportional tothe rate constant, and determine the constant of proportionality.arrow_forwardUnder what conditions might a reaction be endothermic but exergonic? Explain.arrow_forward
- 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. ESarrow_forwardSketch the appropriate plots on the following axes. Assume that simple Michaelis- Menten kinetics apply, and that the pre-steady state occurs so rapidly that it need not be consideredarrow_forwardExamine the reaction below. Using the table of standard state free energies provided: A) Calculate the standard state free energy change for the reaction (in the direction shown). B) Under standard state conditions, will this reaction proceed to the LEFT(down) or RIGHT (up)? AG° (kJ/mol) - 62 NH2 COMPOUND wbydrolysis Phosphoenolpyruvate Creatine phosphate CH2OH - 43 N- - 'N' - 32 - 21 - 14 АТР - ОН Glucose-1-phosphate Glucose-6-phosphate + H OH ОРОЗ H ОН H ОН OH NH2 N. N. CH2OH O-P-0- ОН H + ОН ОН OH ОН ОН |arrow_forward
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