4. If the standard reduction potential for NAD+ to NADH is -0.320 V at pH 7 and the standardreduction potential for two protons to molecular hydrogen at pH 7 is -0.414, what is AG°' for areaction that uses NADH and a proton to produce molecular hydrogen?

Biological oxidation-reduction reactions involve the transfer of electrons from one biomolecule,…

Answered: 4. If the standard reduction potential…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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3.
3. Show the calculation of (1) the expected grams of alum (KAI(SO4)2 12 H2O) formed from the reaction of 1.4 grams of aluminum metal and then show the calculation of (2) the % yield if the actual yield of alum is 21.31 grams. Overall reaction is shown below: 2 Al + 2 KOH + 10 H2O + 4 H2SO4 →2 KAI(SO4)2 12 H2O + 3 H2(g)T
22. For the process, A B, Keq is 0.02 at 37°C. For the process, BC, Keq 1000 at 37°C. A. Determine Keq (AC), the equilibrium constant for the overall process A C, from Keq (AB) and Keq (BC). B. Determine standard-state free energy changes for all three processes and use AG'(AC) to determine Keq (AC). Make sure that this value agrees with that determined in part A of this problem.
Which of the compounds shown below exhibit a high negative free energy of hydrolysis equal to or larger than the free energy of hydrolysis for the phosphoanhydride of ATP? (Choose all that apply) В Α HPΗ Ho HO HO H2N-CH-C CH2 H2N-CH-C CH2 CH2 H2N-CH-Ö CH2 C CH2 D E O A O B O E O=p-00 O=p-00 O=-00 O=0-00 O=L-00
11. Refer to the figure below. нн Н `NH2 NH2 N' N- 2e-+H* R NAD+ NADH NAD+ functions as a coenzyme in many enzyme-catalyzed reactions. The changes that take place in this coenzyme are the same for all of these reactions and are illustrated in the figure. It is likely that, in these reactions, NAD+ functions as an electron acceptor (reducing agent) in redox reactions. functions as an electron donor (oxidizing agent) in redox reactions. functions as a base in acid-base catalytic mechanisms. functions as an electron donor (oxidizing agent) in redox reactions. functions as an electron acceptor (oxidizing agent) in redox reactions. +Z-
2. The Km of a particular enzyme is 2.0 x 105 M. If the initial velocity (Vo) is 0.16 mmol/min for [S] = 0.15 M, what will be the initial velocity when [S] =2.0 x 10+M?
1. A reaction in which a substrate is converted to a product is catalyzed by an enzyme. The reaction was determined to have ket = 10,000. s', KM = 90.0 µM, and a standard Gibbs free energy change of -13.8 kJ mol. Answer the following questions about experiments performed with 2.00 nM enzyme. R= 8.3145 J mol K. !3! a) Calculate the change in free energy for this reaction at room temperature (25.0°C) under the following conditions, and indicate whether the forward reaction is favored or not. i. [(S] = 2.00 µM and [P] = 2.00 nM. !! it. [S] = 2.00 uM and (P) = 2.00 uM.
Calculating ATP Yield 'Assumes an ATP equivalence: 2.5 ATP per NADH and 1.5 ATP per FADH2. * Assumes an ATP equivalence: 3 ATP per NADH and 2 ATP per FADH2. CH3(CH,) COOH ** 1st Formula 2nd Formula Capric Acid (7 x C) - 6 (8.5 x C) -7 Carbons = 10 (7 x 10) - 6 = 64ATP (8.5 x 10) - 7 = 78ATP 1. Palmitic Acid is a saturated long-chain fatty acid with a 16-carbon backbone. It is found naturally in palm oil and palm kernel oil, as well as in butter, cheese, milk and meat. Its chemical formula is CH;(CH2)14COOH. Calculate ATP using the first formula.
6. An enzyme catalyzed reaction has a KM of 1 mM and a Vmax of 5 nM/s. What is the reaction velocity when the substrate concentration is (a) 0.25 mM (b) 1.5 mM, and (c) 10 mM?
You are evaluating the kinetics of an enzyme catalyzed reaction containing 5.5 μM total enzyme and 11.2 μM substrate. At this substrate concentration, you determine that the Vo = 88.6 μmol mL-¹. s-¹. If the Vmax 833.3 mM s the KM is: . == " 30.9 μΜ 10.4 μΜ Ο 124.6 μΜ 234 μΜ 94.5 μM
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
12. Explain why those biological reactions that have their equilibria shifted towards theproducts have negative values for ΔGo of reactions. Explain how equilibria relates toGibbs free energy.

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4. If the standard reduction potential for NAD+ to NADH is -0.320 V at pH 7 and the standard reduction potential for two protons to molecular hydrogen at pH 7 is -0.414, what is AG" for a reaction that uses NADH and a proton to produce molecular hydrogen?