O2 is a competitive inhibitor of the hydrogenase enzyme that catalyzes the conversion between protons & electrons and H2. The inhibition by O2 is irreversible, permanently destroying the enzymatic activity. (a) Describe the relevant reactions that take place when a hydrogenase catalyzes H2 production in the presence of O2. (b) Derive the rate equation for v as a function of [E], [H+] and [O2], assuming that the electron concentration/delivery is not rate-limiting.
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O2 is a competitive inhibitor of the hydrogenase enzyme that catalyzes the conversion between protons & electrons and H2. The inhibition by O2 is irreversible, permanently destroying the enzymatic activity.
(a) Describe the relevant reactions that take place when a hydrogenase catalyzes H2 production in the presence of O2.
(b) Derive the rate equation for v as a function of [E], [H+] and [O2], assuming that the electron concentration/delivery is not rate-limiting.
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- In the beta oxidation of linoleic acid, converting the 3, 5, 8 trienoyl CoA intermediate back to an expected intermediate for a beta oxidation substrate costs the equivalent of how many ATPs? (hint: look at the 'right side' of the figure for addressing problem 3 with linoleic acid)Indicate whether each of the following changes represents oxidation or reduction. Write: O = for oxidation ; R= for reduction Example: cyt ci (Fet) → cyt c1 (Fe2+) Answer: R Blank #1: COQH2 → CoQ Blank #2: NAD+ - NADH Blank #3: FMN → FMNH2 Blank # 4: FADH2 FAD Blank #5: Fe(III) SP → Fe(II) SP Blank # 1 Blank # 2The phosphorylation of glucose to glucose 1-phosphate requires 5.0 kcal/mol of energy. This unfavorable reaction can be driven by the hydrolysis of ATP to ADP. (a) Write the equation for the coupled reaction. (b) How much energy is released in the coupled reaction? glucose + HPO4---------->2– glucose 1-phosphate + H2O
- Discuss the relationship between redox potentials E0’ and the organization of the components of the electron transport chain. Be specific, i.e., use data/actual values to back up your discussion. a) What are the values of E0’ for all the components of the ETS? b)How are the E0’ related to ∆G values? c) How do the values of E0’ vary among the participants in the ETS relative to their position in the ETS?a) Based on the data shown in the image, what are the Km and Vmax for the enzyme with L-DOPA and D-DOPA? Show any relevant analyses or calculatins you did to determine these values. ( HINT a graph might be helpful here! ) b) Based on your answer to part a, briefly describe how the kinetics of the enzyme differs for the two substrates. Which Substrate has better binding affinity to the enzymeWhich of the following statements is true about the chymotrypsin reaction? 1. The catalytic triad at the active site is formed by three residues: His, Gly, and Ser 2. When the substrate is p-Nitrophenylacetate, the rate-limiting step is the release of p-Nitrophenolate. 3. During the reaction, LBHB forms when the proton is donated to His from Ser or water. 4. The chymotrypsin reaction involves “only” specific acid-base catalysis 5. The “oxyanion hole” is formed by the amide nitrogens of Ser and Glu
- When pure reduced cytochrome c is added to carefully prepared mitochondria along with ADP, Pi, antimycin A, and oxygen, the cytochrome c becomes oxidized, and ATP is formed, with a P/O ratio approaching 1.0.(a) Indicate the probable flow of electrons in this system.(b) Why was antimycin A added?(c) What does this experiment tell you about the location of coupling sitesfor oxidative phosphorylation?(d) Write a balanced equation for the overall reaction (including cyt c oxidation and ATP synthesis).(e) Calculate ΔG°′ for the above reaction, using E′0 values from Table 14.1and a ΔG°′ value for ATP hydrolysis of -32.2 kJ/mol.The inhibitor X prevents coenzyme Q (Q) from participating in electron transfer in the electrontransport chain.(a) Will the presence of X prevent electrons from N ADH from passing through the electron trans-port chain? Explain why or why not.(b) Compound Y is a non-physiological reducing agent capable of directly reducing cytochromec1 in Complex III. Would oxygen consumption resume upon the addition of compound Y tomitochondria inhibited by inhibitor X? Be sure to explain your answer.Compound X is an inhibitor in respiratory electron transfer. It binds to the Fe3+ of Complex IV preventing oxygen binding. (a) Suggest an example of compound X. (b) How would compound X affect the NADH / NAD+ ratio? Explain briefly. (d) Given: Complexes II, III and IV, cytochrome c, Q, succinate and compound X Draft the ELECTRON FLOW and determine the FINAL ELECTRON ACCEPTOR with explanation under AEROBIC condition.
- The complete oxidation of palmitoyl-CoA to carbon dioxide and water is presented by the overall equation: Palmitoyl-CoA + 23O2 + 108Pi + 108 ATP + 23H2O → CoA + 16 CO2 + 108 ATP + 23H2O Water is also produced in the reaction ADP + Pi → ATP + H2O But not included as a product in the overall equation. Why?Starting with glucose, there are five steps in the EMP/TCA metabolic pathways that produce NADH (which is converted to ATP or energy). Use class notes, Shuler, Kargi and DeLisa book, or the internet. 1. A. Draw the chemical structures of the reactant(s) and product(s); as well as a balanced chemical reaction for the step in the TCA (Krebs) cycle where isocitrate is converted to a-ketoglutarate (step 3 in the class notes). (You don't need to draw the structures of coenzyme A (COA), NAD* or NADH.) B. What enzymes catalyze steps 3 and 5 in the Kreb's cycle from the class notes? C. Would you categorize step 8 in the TCA cycle where malate is converted to oxaloacetate as an oxidation or reduction of malate? D. Considering that some energy is spent transporting acetyl-CoA to mitochondria, how much net energy (in kcal) is produced by converting 15 mol of glucose to CO₂ in the glycolysis & Krebs cycle pathways? E. How many kcals of energy from oxidizing 15 mol of glucose to CO₂ (your answer to…The following nutrient molecule is digested and transported to a cell where it undergoes further catabolism: H- OH H OH OH CHOH In the table below, list the important products of the complete B oxidation of this molecule. • In the first column of the table, write the chemical formula, name, or standard blochemical symbol for a product molecule. In the second column, write the total number of these molecules produced. • Only list the important products, Including (1) molecules with any of the carbon atoms that were in the eriginal molecule, (2) energy storage molecules (ike ATP), and (3) newly oxidized or reduced coenzymes. • List each product molecule on a separate row. You can add more rows if you need them. • Be sure you write the number of product molecules formed by the complete p oxidation of the molecule above. • Do not include the products of any catabolic activity that happens before or after oxidation, including any necessary activation. f the molecule contains small parts…