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- 1. Cyanide, oligomycin, and 2,4-dinitrophenol are all inhibitors of oxidative phosphorylation in mitochon- dria. Provide an explanation to the following conditions regarding these potent inhibitors. (a) Explain why adding cyanide to an active in vitro suspension of mitochondria blocks ATP synthesis. What happens to the rate of ATP synthesis when 2,4-dinitrophenol is added to this mitochon- drial suspension after it was treated with cyanide? (b) Explain why the rate of oxygen consumption decreases in an in vitro suspension of mito- chondria when oligomycin is added. What happens to the rate of oxygen consumption in this oligomycin- inhibited system after adding 2,4-dinitrophenol? Explain.1. The first step in the payoff phase of glycolysis is catalyzed by the enzyme glyceraldehyde 3-phosphate dehydrogenase, an enzyme that contains a nucleophilic cysteine playing a central role in the reaction. A) In the direction of gluconeogenesis, what reaction does this enzyme catalyze? AG° = -6.3 kcal/mol for this reaction in the direction of gluconeogenesis. Based on what you know about the substrates involved, provide two chemical reasons as to why the AGO of this reaction is negative.1. (a) The reaction catalyzed by citrate synthase is the first step of the TCA cycle. In glycolysis, two key reactions to produce ATP occur because an unfavorable reaction is coupled to another reaction that is thermodynamically favorable. The reaction catalyzed by citrate synthase is similarly coupled to an unfavorable reaction in the TCA cycle. Write the unfavorable TCA reaction using structural formulas and write the key step that drives the two coupled reactions forward. What is the overall AG" of the coupled reactions? (b). K(yM) 25.7 Inhibitor Bromoacetyl-CoA ATP NADH 6800 8300 The inhibitor constants for three inhibitors of por- cine citrate synthase are summarized in the table on the right. The compounds were all determined to bind in the ac- tive site as competitive inhibitors of acetyl-CoA. Because they bind as competitive inhibitors, all three inhibitors must exhibit structural similarity to some part of acetyl-CoA. Look up in the textbook the structural formulas for…
- 4. As stated in your textbook, the first two reactions in glycolysis associated with unfavorable AG° values, i.e., AG° > 0, both produce a product with high phosphoryl group transfer potential. (ATP formation is not considered here.) Compare the two reactions and describe what the driving force is for both reactions that allows glycolysis to proceed to formation of pyruvate.the first two reactions in glycolysis associated with unfavorable ∆G° values, i.e., ∆G° > 0, both produce a product with high phosphoryl group transfer potential. (ATP formation is not considered here.) Compare the two reactions and describe what the driving force is for both reactions that allows glycolysis to proceed to formation of pyruvate.3.) As mentioned in the March1 outline a critical step in the glycolysis metabolic pathway (conversion for glucose to pyruvate that produces 2 ATP's) is the attachment of dihydroxyacetone phosphate to an isomerase enzyme via an iminium bridge (step1). There is a second step that takes the imine to the enamine that sets up the C-C formation reaction with an enol that you'll cover in two weeks. Show the mechanism for steps 1 (mild acid catalysis) and 2 (draw resonance forms for the iminium cation). In your mechanism, show the intermediate hemiaminal (carbinolamine). Step 2 may address one of the questions asked in Wednesday's class about the water taking out the N-H proton of the iminium cation versus a C-H proton? CH₂OPO3² E-NH₂ + O=C (step 1) CH₂OH Dihydroxyacetone phosphate Iminium (+) cation intermediate (step 2) Enamine (Enol) Intermediate H CH₂OPO32- E-N-C H C. OH H₂O E
- 2. The overall result of CH,OH + 2 NAD+ + 2 NADH glycolysis can be summarized by the equation on the right in which HO the glucose origins of the carbon atoms in pyruvate are color coded. Show by writing the reactions catalyzed by aldolase and triose phosphate isomerase and num- bering the carbons why this is the fate of glucose carbon atoms in pyruvate. Indicate numbering of carbons in Glucose-6-Pi, Fructose-1,6-BisPi, enzyme products, and pyruvate. HO + 2 Pi 2 + 2 ATP > OH + 2 ADP (CH3 + 2 H20 Glucose Pyruvate6. Malate dehydrogenase catalyzes the following reversible reaction: COO- HO-C-H CH₂ COO™ L-Malate NAD+ y malate NADH + H+ dehydrogenase COO- 0=C CH₂ COO™ Oxaloacetate AG'° = 29.7 kJ/mol Malate + NAD+→NADH + H+ + oxaloacetate Calculate AG" and the ratio or products and reactants for the malate dehydrogenase reaction to proceed from left to right as shown. (The Faraday constant. 3, is 96.48 kJ/V-mol; RT(37°C)= 2.58kJ/mol) Steps: 1. Explain how you determined which molecule is an electron donor Malate and which is an acceptor NAD*. -2- 2. Calculate AED (write equation, then show calculations, for standard reduction potentials (E_values) see table in the posted lecture) 3. Calculate AG (write equation, then show calculations) 4. Calculate the ratio of products and reactants needed to for Malate + NAD+→→NADH + H+ + oxaloacetate reaction to proceed forward (write equation, then show calculations)1. Identify the oxidized coenzyme (letter abbreviation only) that participates in this reaction of the Kreb’s cycle. Succinate --> Fumarate 2. How many mol of NADH can be obtained upon the beta oxidation of stearic acid? 3. How many mol of ATP can be obtained upon the complete oxidation of 1 mol stearic acid? 4. How many steps in glycolysis in which ATO is converted to ADP?
- 2. If glyceraldehyde-3-phosphate dehydrogenase in red blood cells is completely inhibited, which intermediates in glycolysis accumulate most? Please use the following equation and the provided information to explain your reasoning. AG=AG° + RTln [C][D]d [A] [B]¹ Fructose 1,6-bisphosphate → Glyceraldehyde 3-phosphate + Dihydroxyacetone phosphate The standard free energy for the above reaction is: AG" = +23.9 KJ/mol T° = 298 R = 8.314 J mol-¹ K-¹23. An important step in glycolysis is the formation of ATP and pyruvate from phosphoenol-pyruvate (PEP) and ADP. PEP ADP pyruvate+ATP The equilibrium constant (Keq) for this reaction is approximately 2.5x10°. Calculate standard free energy change (AG°') for this reaction. Show your work. onege b. Is the reaction exergonic or endergonic at standard conditions? If, at equilibrium, the concentrations of ADP and ATP are 0.2 mM and 2.0 mM, respectively, what is the equilibrium concentration ratio of [pyruvate] to [PEP]? Show your work. с.2. Please, determine the answers of these multiple choices, they’re in a,b,c’s. A) The role of oxygen in oxidative phosphorylation (cellular breathing) is: -To be the last electron acceptor in the electron transfer chain -To hydrolyse carbohydrates - To add hydrogen ions to pyruvic acid at the end of glycolysis -To provide electrons for NADP reduction -To provide hydrogen ions B) Which molecule has the most potential energy? -glucose -phosphate -fructose 1-6 diphosphate -ethanol -I'ATP C) What is the product of fermentation in yeasts? -carbonic acid -oxygen -ATP -lactic acid -ethanol