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Concept explainers
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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Chapter 20 Solutions
Bundle: Biochemistry, Loose-leaf Version, 9th + Owlv2,1 Term Printed Access Card
- 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 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_forwardMATHEMATICAL 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_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
- BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage Learning
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