Given the following information on reduction potentials, calculate the standard free energy in kJ/mol based on your understanding of electron transfer through the pyruvate dehydrogenase complex. Round to nearest whole number. Lipoamide + 2H+ + 2e- dihydrolipoamide Ae° = -0.29 FAD + 2H+ + 2e- FADH, Aɛ° = -0.01
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- The overall adenylate kinase reaction (2 ADP = AMP + ATP) is a combination of 3 reactions: ATP hydrolysis, pyrophosphate hydrolysis, and ATP formation. Show each step and provide the standard free energy (ΔG°′) for each and the overall reaction. If the adenylate kinase reaction is at equilibrium and intracellular [ATP] = 5 mM and [ADP] = 0.5 mM, calculate the concentration of AMP at pH 7 and 25 °C. Show all work. ATP (ADP+P) = -30.5 kj/mol; ATP (AMP+PP) = -45.6 kj/mol; PP = -19.2 kj/mol1 In relation to the redox below from electron transport chain (SuccinateDehydrogenase) Show calculations that proof how oxidation of FADH2 by ubuiqinone(Q) theroteically liberates enough enrgy to drive synthesis of ATP. △G°‘ or ATP synthesis from ADP and π is +30.5kj/mol. Explain calculation in terms of how the oxidation of FAD Hz by ubiquinone supplies sufficient energy for ATP synthesis from ADP and π.The aconitase-catalyzed addition of water to cis-aconitate in the citric acid cycle occurs with the following stereochemistry. Does the addition of the OH group occur on the Re or Si face of the substrate? What about the addition of the H? Do the H and OH groups add from the same side of the double bond or from opposite sides?
- Assume you are studying a hydrolase that catalyzes the following reaction which has a ΔGO of + 27 kJ/mol. A-B + H2O ↔ A-H + B-O− + H+ a. What is Keq for this reaction? b. What are Keq’ and ΔGO’ for this reaction? c. Is this reaction favorable under standard biochemical conditions at pH 7? Justify your answer.You are called in as a consult for a patient who suffers from acidosis. Urine levels of both lactic acid and isocitric acid are elevated. Mitochondria isolated from the patient’s fibroblasts oxidize pyruvate very slowly whereas α-ketoglutarate and malate are oxidized normally. a. At what enzyme would you predict the patient has a defect? b. Why? What evidence do you have to choose that enzyme? c. How do you account for the increase in lactic acid?A) Assuming that ubiquinone is unavailable inside of the cell, calculate the delta G and the Keq if electrons are transferred directly from complex l to complex lll of the electron transport chain. In your answer include the net equation for this electron transfer. Constants: R = 8.31/ degree1mol, F = 96.1kJ/voltmol, T = 298K. Half reaction: E(V) Ubiquinone + 2e- + 2H+ --> Ubiquinol + H2 0.045 NAD+ + 2e- +2H+ --> NADH + H+ -0.320 1/2 O2 + 2e- + 2H+ --> H2O 0.816 Cytc (Fe3+) + + 1e- + 1H+ --> Cytc (Fe3+) 0.254 B) In a single sentence explain whether or not this electron transfer is possible
- please please help me to answer it >>> i have an exam Human xanthine oxidase catalyzes the oxidation of hypoxanthine to xanthine and can furthercatalyze the oxidation of xanthine to uric acid. For the treatment of hyperuricemia and gout,several medications are used to inhibit the activity of xanthine oxidase and reduce theproduction of uric acid. You are a biochemist and just discovered a chemical that can inhibitthe activity of the human xanthine oxidase. When analyzing its mode of inhibition, you foundthat the enzyme inhibitor complex requires 450 J.mol-1 to dissociate and that it displayskinetics somehow similar to noncompetitive inhibition. You sent your inhibitor to the ministryof health for approval as a medication for gout. Based on the data provided, are they going toauthorize it as a medication or not? Explain?Explain, using Le Châtelier’s principle, why the equilibriumconstant for the formation of NO from N2 and O2increases with increasing temperature, whereas the equilibriumconstant for the formation of NO2 from NO and O2decreases with increasing temperature.The thiamine pyrophosphate (TPP)-dependent enzyme benzoylformate decarboxylase catalyzes the decarboxylation of benzoylformate to yield benzaldehyde. Propose a mechanism based on your knowledge of TPP-dependent mechanisms. You may begin the reaction with the ylid form of TPP and you only need to show the structure of the “business end” of TPP. Show all electron flow using the arrow convention.
- The vitamin Niacin is used to form nicotinamide adenosine dinucleotide, which readily shuttles between its oxidized (NAD+) and reduced (NADH) forms. The latter serves as a cellular equivalent to NaBH4. The essential portions of the structures are shown below. Outline a mechanism for the cellular conversion of pyruvate to lactate. (Note: like NaBH4, NADH cannot reduce carboxylic acid carbonyls).Which of the reactions are spontaneous (favorable)? 1)DHAP↽−−⇀glyceraldehyde-3-phosphateΔ?=3.8 kJ/mol 2)L-malate+NAD+⟶oxaloacetate+NADH+H+Δ?=29.7 kJ/mol- 3) glutamate+NAD++H2O⟶NH+4+α-ketoglutarate+NADH+H+Δ?=3.7 kcal/ 4) C6H13O9P+ATP⟶C6H14O12P2+ADPΔ?=−14.2KJ/mol 5) −Rh(I)C2H6Δ?=−150.97 kJ/molC2H4+H2→Rh(I)C2H6ΔG=−150.97 kJ/mol 6) C4H4O5⟶C4H2O4+H2OΔ?=3.1 kJ/molwhat is the sterochemical outcome and draw the transition state responsible for steroinduction. -draw clearly