Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
expand_more
expand_more
format_list_bulleted
Question
Chapter 18, Problem 13P
Interpretation Introduction
Interpretation:
Relation between free energy change and redox potential.
Concept introduction:
The redox potential is the measure of the tendency of any chemical compound to lose or accept electrons and attain an oxidized or reduced state. The electrode potential of a compound to accept an electron is termed as reduction potential. Further, the oxidation potential is the potential of the compound on losing its electrons
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
6-25
substrate-band enzyme concentrations. The the
turnover number is equal to umax-
b)
V=Umax •57(Km+S)
anstont
For an enzyme that displays Michaelis-Menten kinetics, what is
the reaction velocity, V (as a percentage of Vmax), observed at
the following values?
a)
[S] = KM
C)
d)
e)
[S] = 0.5KM
[S] = = 0.1KM
[S] = 2KM
[S] = 10KM
w
reactores
-maximumrate of reaction
boteles conc.
Would you expect the structure of a competitive inhibitor of a
given enzyme to be similar to that of its substrate?
Select the incorrect statement. With regards to free energy ΔG of the reaction below
E+S ⇌ ES
Negative ΔG mean the reaction toward is facourable
More negative value of ΔG indicates stronger binding to S to E
It is possible to compute disassociation constant from the ΔG value alone
It is possible to calculate the term ( ΔH – T ΔS) from the value of ΔGalone
ΔG = 0 indicates (ES)/(E)(S) =1
None of the above
ch
Select all statements that are correct. Note there might be more than 1 correct
statement.
From the Lineweaver-Burk plot the equilibrium constant (Keq) can be obtained
The Lineweaver-Burk plot gives a more accurate prediction for Vmax than the Michaelis-
Menten plot
The Lineweaver-Burk plot assumes that products and reactants are present at equal
concentrations during the entire time of the reaction
The Lineweaver-Burk plot shows velocity of reaction vs substrate concentration
The Lineweaver-Burk plot shows 1/velocity of reaction vs 1/substrate concentration
O
20°C
D)
//
E
Chapter 18 Solutions
Biochemistry
Ch. 18 - Prob. 1PCh. 18 - Prob. 2PCh. 18 - Prob. 3PCh. 18 - Prob. 4PCh. 18 - Prob. 5PCh. 18 - Prob. 6PCh. 18 - Prob. 7PCh. 18 - Prob. 8PCh. 18 - Prob. 9PCh. 18 - Prob. 10P
Ch. 18 - Prob. 11PCh. 18 - Prob. 12PCh. 18 - Prob. 13PCh. 18 - Prob. 14PCh. 18 - Prob. 15PCh. 18 - Prob. 16PCh. 18 - Prob. 17PCh. 18 - Prob. 18PCh. 18 - Prob. 19PCh. 18 - Prob. 20PCh. 18 - Prob. 21PCh. 18 - Prob. 22PCh. 18 - Prob. 23PCh. 18 - Prob. 24PCh. 18 - Prob. 25PCh. 18 - Prob. 26PCh. 18 - Prob. 27PCh. 18 - Prob. 28PCh. 18 - Prob. 29PCh. 18 - Prob. 30PCh. 18 - Prob. 31PCh. 18 - Prob. 32PCh. 18 - Prob. 33PCh. 18 - Prob. 34PCh. 18 - Prob. 35PCh. 18 - Prob. 36PCh. 18 - Prob. 37PCh. 18 - Prob. 38PCh. 18 - Prob. 39PCh. 18 - Prob. 40PCh. 18 - Prob. 41PCh. 18 - Prob. 42PCh. 18 - Prob. 43PCh. 18 - Prob. 44PCh. 18 - Prob. 45PCh. 18 - Prob. 46PCh. 18 - Prob. 47PCh. 18 - Prob. 48PCh. 18 - Prob. 49PCh. 18 - Prob. 50PCh. 18 - Prob. 51PCh. 18 - Prob. 52PCh. 18 - Prob. 53PCh. 18 - Prob. 54PCh. 18 - Prob. 55PCh. 18 - Prob. 56PCh. 18 - Prob. 57PCh. 18 - Prob. 58PCh. 18 - Prob. 59P
Knowledge Booster
Similar questions
- YA *H 23. Write free energy change (AG), standard free energy change (AG), and biochemical free energy change conditions (AG") (leave blank if something doesn't apply to the condition) Temperature Pressure Reactant's initial conc. [H+] conc. [H₂O] Free energy change standard free energy (AG) change (AG") Biochemical standard free energy change (AGI)arrow_forwardQ.1 -8 K» for HCO3 = 2.38 × 10 Calculate Ka for the conjugate acid ( H¿CO;) For the reaction : H2CO3(aq) + H2O(aq) HCO3'(aq) + H3Oʻ(aq)arrow_forwardAn enzyme has a rate enhancement of 1.3x106. Calculate the value of ΔΔG‡ at 25.0 °C in kJ mol-1. (Hint: be sure to pay attention to units and signs.) (R = 8.3145 J mol-1 K-1)arrow_forward
- Please balance the reaction below. Considering the pe0 of Pb2+/Pb0 and O2/H2O are -2.13 and 14.5, respectively, will the oxidation of Pb0 by oxygen occur under conditions: pH 8, [Pb2+] = 5x10-8 M, [O2(aq)] = 2.5x10-4 M? Pb0 + O2 + H+ → Pb2+ + H2Oarrow_forward2c which is altered by a catalyst such as an enzyme, the net free energy change of the reaction or the activation energy of the reaction?arrow_forwardEnzyme X exhibits maximum activity at pH- 6.3. X shows a fairly sharp decrease in its activity when the pH goes much lower than 5.8. One likely interpretation of this pH activity is that: a Glu residue on the enzyme is involved in the reaction. O the enzyme uses NADH has a cofactor the enzyme uses coenzyme A has a cofactor O a Tyr residue on the enzyme is involved in the reaction. O a His residue on the enzyme is involved in the reactionarrow_forward
- At 300 K, what fold improvement in a reaction rate do you expect if AG* is brought down from 40 kJ/mol to 20 kJ/mol, without changing of the reaction mechanism, as a result of enzymatic catalysis? е. f. there will be (1) no effect, (2) an increase, or (3) a decrease? The following may or may not be affected by the addition of an enzyme to a chemical reaction. State if A) activation energy of the reaction B) standard free energy of the reaction C) time to reach equilibrium D) equilibrium constant of the reaction E) initial velocity of the reaction g. Remember the simple kinetic mechanism for an enzyme-catalyzed reaction. It was reported that the rate-limiting step is the following reaction k2 ES > P Under these circumstances, the Michaelis constant becomes equivalent to A) [S], when Vo = Vmax B) Turnover number C) Specificity constant D) kcat E) the dissociation constant for the Enzyme-Substrate (ES) complexarrow_forwardEnzyme X exhibits maximum activity at pH = 6.3. X shows a fairly sharp decrease in its activity when the pH goes much lower than 5.8. One likely interpretation of this pH activity is that: a Glu residue on the enzyme is involved in the reaction. a Tyr residue on the enzyme is involved in the reaction. a His residue on the enzyme is involved in the reaction the enzyme uses NADH has a cofactor. the enzyme uses coenzyme A has a cofactor.arrow_forwardΔG°′ for the isomerization reaction glucose-1-phosphate (G1P) ⇌ glucose-6-phosphate (G6P) is −7.1 kJ · mol−1. Calculate the equilibrium ratio of [G1P] to [G6P] at 25°C.arrow_forward
- O BIOCHEMISTRY Understanding major biochemical energy storage and release. A certain anabolic biochemical reaction A has AG- 17.8 kJ mol , and is always coupled to another reaction B, which has two reactants and two products, I this: R + R2 P + P2 The molecule in the drawing area below is either R, or P. • If it's R, change it into P. But if it's P, change it into R. • In either case, draw the molecule as it would exist at physiological pH. • Also please answer the questions about Reaction B in the table below. OR, Was the molecule in the drawing area R, or P, before you changed it? What is R? Enter its common name, usual symbol, or chemical formula: What is P2? Enter its common name, usual symbol, or chemical formula: O BIOCHEMISTRY Understanding major biochemical energy storage and release.. ODO its common name, usual symbol, or chemical formula: NH, -CH N. H OH OH ...... to IIIarrow_forwardBe sure to answer all parts. Calculate the equilibrium constants for decomposition of the following hydrogen halides at 298 K. Enter your answers in scientific notation. (a) 2HF(g) H2(g) + F2(g) 0.5 x 10 -97 (b) 2HCl(g) H2(g) + Cl2(g) 3.8 LOL -34 (c) 2HBr(g) H2(g) + Br2(g) 4.9 LO -20 (d) 2HI(g) H2(g) + I2(g) 1.1 -3arrow_forwardOH affromah. The Standard free energy CAGO¹) of the reaction shown above can be estimated based on? OH A. High Energy bands B. Reduction potential C. cannot be estimated OH energy. он The reaction shown above requires the cofactor to proceed forward without significant was te of A.ATP B. Nicotinamide C. Flavin D. No cofactor required 3 Determine approximate 46°1 of the coupled reaction KJ/mol possible answers: (0,-8,-15,-22,-30, -38,-45) The class of enzyme that catalyzes the reaction is possible answers: Mutase, Isomerase, ki nase, phosphatase, Dehydrogenase, Aidolasearrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Cengage Learning