**Question 21:**Which two of the following contribute to the large negative free energy change upon hydrolysis of "high energy" compounds? (There may be more than one correct answer.)- [ ] Stabilization of reactants by ionization- [ ] Stabilization of products by extra resonance forms- [ ] Electrostatic repulsion in the reactant- [ ] A low activation energy of the forward reaction*Note: Moving to another question will save this response.*

Hydrolysis of high energy compounds release energy as hydrolysis involve the breaking of bonds that…

Answered: Question 21 Which two of following…

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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Only do parts d, e, and f
Which of the following is NOT TRUE about allostery?
Please answer fast The equilbrium constant (Keq) under standard conditions for the hydrolysis of ATP is 200,000 M. This would suggest the reaction is: 1. proceeding in reverse direction 2. proceeding in forward direction 3. in equilibrium However, this does not take into consideration the concentration of substrates/products within the cell. This is can be calculated by determining the reaction quotient, Q by: [ATP] x [Pi] / [ADP] [ATP] + [Pi] / [ADP] [ADP] x [ATP] / [Pi] [ADP] x [Pi] / [ATP] Biochemical reactions commonly involve the transfer of groups from ATP. What is one of the products of pyrophosphate cleavage from ATP? AMP Adenosine ADP Inorganic phosphate Q5-6. The hydrolysis of ATP is often coupled to other reactions. For example: Phosphoenolpyruvate (PEP) + H2O → Pyruvate + Pi (ΔG'° = -63.1 kJ/mol) ATP + H2O → ADP + Pi (ΔG'° = -30.5 kJ/mol) (The standard free-energy changes for the reactions are indicated in brackets) Q5. Given the information above, what is the…
I need Question 40
Question 5 Which of the following correctly describes the linkages found in ATP? A one anhydride, two esters and a glycosidic bond B three anhydrides, a phospho ester and a glycosidic bond two anhydrides, two phospho esters and a glycosidic bond two anhydrides, a phospho ester and a glycosidic bond
Incorrect Question 5 The active site of a protein has a shape that most nearly fits None of the above Substrates Products Transition state
8
Question 3 of 13 Fill in the blanks: Write Cif only statement A is correct, Hif only statement B is correct, Eif both statements are correct, Mif both statements are incorrect. A. A lower KM reflects a less efficient enzyme. B. The KM is equivalent to the substrate concentration at 50% of the reaction's velocity limit.
This reaction an enzymatic and reaction has kinetic constants k1, k-1, and k2 were found to be 107 M/s, 4.1-104/s1, and 10²-s1, E+ P What is Km? E+S ES
Question 1: The amount of energy effectively stored in each ATP (the actual energy of ATP hydolysis) will depend on the concentrations of ATP, ADP, and Pi, according to equations discussed in class and in the book. If the ATP synthase is operating at close to equilibrium (as might be the case if ATP is being used slowly), we can compute the maximum possible energy of ATP hydrolysis by assuming balance between the energy provided by the proton gradient and the energy used to make the ATP. (Since we care about the magnitude of the energy it’s convenient to talk in terms of absolute values; the maximum possible ATP hydrolysis energy is then the most negative value possible.) Using what you know about the mechanism of the ATP synthase, and assuming that the membrane gradient consists of a Δψ of -.15V and a ΔpH of 1 unit (alkaline inside), compute the maximum possible ATP-hydrolysis energies for synthases with: a.) 8 c-subunits b.) 13 c-subunits
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
Question 1 (a,b,C)

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