Biochemistry
9th Edition
ISBN: 9781305961135
Author: Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher: Cengage Learning
expand_more
expand_more
format_list_bulleted
Concept explainers
Videos
Textbook Question
Chapter 20, Problem 43RE
REFLECT AND APPLY Criticize the following statement: “The role of the proton gradient in chemiosmosis is to provide the energy to phosphorylate ADP.”
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
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...
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- REFLECT AND APPLY Would nature rely on the same enzyme to catalyze a reaction either way (forward or backward) if the DG were 0.8kcalmol1? If it were 5.3kcalmol1?arrow_forwardREFLECT AND APPLY What is the relationship between a transition-state analog and the induced-fit model of enzyme kinetics?arrow_forwardREFLECT AND APPLY Suggest a reason why heating a solution containing an enzyme markedly decreases its activity. Why is the decrease of activity frequently much less when the solution contains high concentrations of the substrate?arrow_forward
- REFLECT AND APPLY The enzyme D-amino acid oxidase has a very high turnover number because the D-amino acids are potentially toxic. The KM for the enzyme is in the range of 1 to 2 mM for the aromatic amino acids and in the range of 15 to 20 mM for such amino acids as serine, alanine, and the acidic amino acids. Which of these amino acids are the preferred substrates for the enzyme?arrow_forwardREFLECT AND APPLY Why can we say that having a pure non- competitive inhibitor present is similar to just having less enzyme present?arrow_forwardREFLECT AND APPLY Comment on the energetics of protein folding in light of the information in this chapter.arrow_forward
- REFLECT AND APPLY Would you expect an irreversible inhibitor of an enzyme to be bound by covalent or by non-covalent interactions? Why?arrow_forwardREFLECT AND APPLY A model is proposed to explain the reaction catalyzed by an enzyme. Experimentally obtained rate data fit the model to within experimental error. Do these findings prove the model?arrow_forwardREFLECT AND APPLY When we compare the binding of I and of S to the enzyme in a mixed noncompetitive inhibitor, we assumed that the binding of I decreased the affinity of the enzyme for S. What would happen if the opposite were true?arrow_forward
- REFLECT AND APPLY Suggest a reason why the cell membranes of bacteria grown at 20C tend to have a higher proportion of unsaturated fatty acids than the membranes of bacteria of the same species grown at 37C. In other words, the bacteria grown at 37C have a higher proportion of saturated fatty acids in their cell membranes.arrow_forwardREFLECT AND APPLY Noncompetitive inhibition is a limiting case in which the effect of binding inhibitor has no effect on the affinity for the substrate and vice versa. Suggest what a LineweaverBurk plot would look like for an inhibitor that had a reaction scheme similar to that on page 159 (noncompetitive inhibition reaction), but where binding inhibitor lowered the affinity of EI for the substrate.arrow_forwardREFLECT AND APPLY Sulfanilamide and related sulfa drugs were widely used to treat diseases of bacterial origin before penicillin and more advanced drugs were readily available. The inhibitory effect of sulfanilamide on bacterial growth can be reversed by p-aminobenzoate. Suggest a mode of action for sulfanilamide.arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Cengage Learning
Biomolecules - Protein - Amino acids; Author: Tutorials Point (India) Ltd.;https://www.youtube.com/watch?v=ySNVPDHJ0ek;License: Standard YouTube License, CC-BY