Biochemistry
9th Edition
ISBN: 9781305961135
Author: Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher: Cengage Learning
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Chapter 20, Problem 9RE
Interpretation Introduction
Interpretation:
The overall voltage of the given biological reaction is to be determined.
Concept introduction:
Oxidation is the addition of an electronegative element or the removal of an electropositive element in a
The reduction is the addition of an electropositive element or the removal of an electronegative element in a chemical reaction
The chemical reaction in which oxidation process and reduction process takes place and reduction take place simultaneously is called a
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Please show work/answer for 1 (a-c)
Initial rate data for an enzyme that obeys Michaelis–Menten kinetics areshown in the following table. When the enzyme concentration is 3 nmolml-1, a Lineweaver–Burk plot of this data gives a line with a y-intercept of0.00426 (μmol-1 ml s). (a) Calculate kcat for the reaction.(b) Calculate KM for the enzyme.(c) When the reactions in part (b) are repeated in the presence of 12 μM ofan uncompetitive inhibitor, the y-intercept of the Lineweaver–Burk plotis 0.352 (μmol-1 ml s). Calculate K′I for this inhibitor.
Chapter 20 Solutions
Biochemistry
Ch. 20 - RECALL Briefly summarize the steps in the electron...Ch. 20 - RECALL Are electron transport and oxidative...Ch. 20 - Prob. 3RECh. 20 - REFLECT AND APPLY Show how the reactions of the...Ch. 20 - REFLECT AND APPLY How does mitochondrial structure...Ch. 20 - Prob. 6RECh. 20 - Prob. 7RECh. 20 - MATHEMATICAL Using the information in Table 20.2,...Ch. 20 - Prob. 9RECh. 20 - Prob. 10RE
Ch. 20 - MATHEMATICAL Calculate E for the following...Ch. 20 - Prob. 12RECh. 20 - MATHEMATICAL Which is more favorable...Ch. 20 - REFLECT AND APPLY Comment on the fact that the...Ch. 20 - RECALL What do cytochromes have in common with...Ch. 20 - RECALL How do the cytochromes differ from...Ch. 20 - RECALL Which of the following does not play a role...Ch. 20 - Prob. 18RECh. 20 - Prob. 19RECh. 20 - REFLECT AND APPLY Two biochemistry students are...Ch. 20 - REFLECT AND APPLY Cytochrome oxidase and...Ch. 20 - Prob. 22RECh. 20 - REFLECT AND APPLY Reflect on the evolutionary...Ch. 20 - REFLECT AND APPLY Experimental evidence strongly...Ch. 20 - Prob. 25RECh. 20 - REFLECT AND APPLY What is the advantage of having...Ch. 20 - REFLECT AND APPLY Why do the electron-transfer...Ch. 20 - Prob. 28RECh. 20 - Prob. 29RECh. 20 - Prob. 30RECh. 20 - RECALL Describe the role of the F1 portion of ATP...Ch. 20 - Prob. 32RECh. 20 - Prob. 33RECh. 20 - Prob. 34RECh. 20 - REFLECT AND APPLY What is the approximate P/O...Ch. 20 - REFLECT AND APPLY Why is it difficult to determine...Ch. 20 - REFLECT AND APPLY What are some of the...Ch. 20 - RECALL Briefly summarize the main arguments of the...Ch. 20 - Prob. 39RECh. 20 - Prob. 40RECh. 20 - Prob. 41RECh. 20 - Prob. 42RECh. 20 - REFLECT AND APPLY Criticize the following...Ch. 20 - Prob. 44RECh. 20 - Prob. 45RECh. 20 - Prob. 46RECh. 20 - RECALL How does the yield of ATP from complete...Ch. 20 - REFLECT AND APPLY The malate-aspartate shuttle...Ch. 20 - MATHEMATICAL What yield of ATP can be expected...Ch. 20 - MATHEMATICAL The free-energy change (G) for the...
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- MATHEMATICAL Calculate the net ATP yield from oleic acid (18:19). Hint: Remember the step that bypasses acyl-CoA dehydrogenase.arrow_forwardMATHEMATICAL For an enzyme that displays MichaelisMenten kinetics, what is the reaction velocity, V (as a percentage of Vmax), observed at the following values? (a) [S]=KM (b) [S]=0.5KM (c) [S]=0.1KM (d) [S]=2KM (e) [S]=10KMarrow_forwardMATHEMATICAL If a reaction can be written AB, and the G is 20kJmol1, what would the substrate/product ratio have to be for the reaction to be thermodynamically favorable?arrow_forward
- REFLECT AND APPLY The enzyme lactate dehydrogenase catalyzes the reaction Pyruvate+NADH+H+lactate+NAD+ NADH absorbs light at 340 nm in the near-ultraviolet region of the electromagnetic spectrum, but NAD1 does not. Suggest an experimental method for following the rate of this reaction, assuming that you have available a spectrophotometer capable of measuring light at this wavelength.arrow_forwardMATHEMATICAL The standard free-energy change for the reaction Arginine+ATPPhosphoarginine+ADP is +1.7kJmol1. From this information and that in Table 15.1, calculate the G for the reaction Phosphoarginine+H2OArginine+Piarrow_forwardMATHEMATICAL Calculate the ATP yield for the complete oxidation of one molecule of palmitic acid (16 carbons). How does this figure differ from that obtained for stearic acid (18 carbons)?arrow_forward
- MATHEMATICAL Using the data in Table 15.1, calculate the value of G for the following reaction. Creatinephosphate+GlycerolCreatine+Glycerol-3-phosphate Hint: This reaction proceeds in stages. ATP is formed in the first step, and the phosphate group is transferred from ATP to glycerol in the second step.arrow_forwardMATHEMATICAL For the Vmax obtained in Question 26, calculate the turnover number (catalytic rate constant) assuming that 131024mol of enzyme were used.arrow_forwardMATHEMATICAL The enzyme -methylaspartase catalyzes the deamination of -methylaspartate [V. Williams and J. Selbin, J. Biol. Chem. 239, 1636 (1964)]. The rate of the reaction was determined by monitoring the absorbance of the product at 240 nm(A240). From the data in the following table, determine KM for the reaction. How does the method of calculation differ from that in Questions 26 and 27?arrow_forward
- MATHEMATICAL Using the information in Table 20.2, calculate G for the following reaction: 2Cytaa3[oxidized;Fe(III)]+2Cytb[reduced;Fe(II)]2Cytaa3[reduced;Fe(II)]+2Cytb[oxidized;Fe(III)]arrow_forwardMATHEMATICAL For the following aspartase reaction (see Question 28) in the presence of the inhibitor hydroxymethylaspartate, determine KM and whether the inhibition is competitive or noncompetitive. [s](molarity)V,noInhibitor(arbitraryunits)V,InhibitorPresent(samearbitraryunits)110451041.5103510311.00.0260.0920.1360.1659.520.0100.0400.0860.1427.60arrow_forwardKinetic Parameters of Enzyme-Catalyzed Reactions TABLE 12-1 The Values of KM, Keat, and Keat/KM for Some Enzymes and Substrates Enzyme Substrate KM (M) 9.5 x 10-5 1.2 x 10-² 2.6 x 10-2 2.5 x 10-2 4.4 x 10-1 8.8 x 10-2 6.6 x 10-4 Acetylcholinesterase Carbonic anhydrase Catalase Chymotrypsin Fumarase Urease Acetylcholine CO₂ HCO₁ H₂O₂ N-Acetylglycine ethyl ester N-Acetylvaline ethyl ester N-Acetyltyrosine ethyl ester Fumarate Malate Urea 5.0 x 10-6 2.5 x 10-5 2.5 x 10-2 Keat (S-¹) 1.4 x 104 1.0 × 106 4.0 × 105 1.0 X 107 5.1 x 10-2 1.7 × 10-1 1.9 X 10² 8.0 x 10² 9.0 × 10² 1.0 X 104 Keat/KM (M¹s¹) 1.5 × 108 8.3 x 107 1.5 x 107 4.0 X 108 1.2 x 10-1 1.9 2.9 × 105 1.6 × 108 3.6 X 107 4.0 X 105 Which enzyme is the most catalytically efficient? Which substrate does chymotrypsin bind to most tightly (assume k_₁ >> K₂)? Is fumarate or malate a better substrate of fumarase? Is it possible to have a kcat/KM of greater than 1 x 10⁹ M-¹ s-¹? Why or why not?arrow_forward
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