Indicate whether each of the following changes represents oxidation or reduction.
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- Consider oleic acid (18:1∆9): 1. How many NADH will be produced from complete oxidation of this fatty acid? 2. How many FADH2 will be produced from complete oxidation of this fatty acid? 3. Total number of ATP produced from NADH in complete oxidation of oleic acid (exclude transport cost of the fatty acid)? 4. Total number of ATP produced from FADH2 in complete oxidation of oleic acid (exclude transport costs of the fatty acid)? Please provide how you got them.Consider the typical beta oxidation of linoleic acid (C18:2 ^Δ9, 12): How many ATP are generated in complete oxidation of linoleic acid? How many NADH are generated in complete oxidation of linoleic acid? How many FADH2 are generated in complete oxidation of linoleic acid?The glutamate dehydrogenase (GDH) catalyses the following reaction: H +H₂N- -C -COO CH₂ CH₂ COO™ acide glutamique + NAD + H₂O GDH Time (min) A340 COO™ c=o CH₂ 5 1 2 3 4 1.760 1.718 1.675 1.635 1.595 CH₂ COO + NH4+ NADH + H+ acide a-cétoglutarique The activity of GDH is monitored in the sense of the formation of glutamate using the following conditions: 0.2 mL of 5 M ammonium sulphate 2.4 mL of buffer at pH 8 0.1 mL of NADH at 6.15 mg.mL-¹ (M = 709 g.mol-¹) 0.2 mL of 1 M a-ketoglutarate solution Warm mixture at 25 °C for 5 min Add 0.1 mL of GDH solution containing 1.6 mg.mL-¹protein to start the reaction. The change in absorbance at 340 nm is monitored, in a 1-cm cuvette, every minute for 10 min. Results are given in the table below: Data ENADH at 340 nm = 6220 M¹.cm7 6 7 8 9 10 1.550 1.510 1.489 1.476 1.451 Calculate ammonium sulphate, NADH, concentrations in the reaction medium at t = 0. proteins - Draw the graph A = f(t). Calculate A340 at t = 0 and place this point on the curve. -…
- Under standard conditions, will the following reactions proceed spontaneously as written? (1) Fumarate + NADH + H+ (2) succinate + NAD+ Cyto a (Fe²+) + cyto b (Fe³+) = cyto a (Fe³+) + cyto 6 (Fe²+) bComplete the sentence describing the pentose phosphate pathway in cells that require much more ribose 5-phosphate than NADPH. These cells need ribose 5-phosphate but have relatively higher concentrations of NADPH and lower concentrations of NADP*. Choose from the listed words to fill in the blanks: xylulose 5-phosphate, fructose 6-phosphate, glucose 6-phosphate, five, two, three, glyceraldehyde 3- phosphate, erythrose 4-phosphate, sedoheptulose 7-phosphate. One molecule of and two molecules of are used to generate molecules of ribose 5-phosphate by the reverse reactions of the nonoxidative phase of the pentose phosphate pathway.(a) Consider the oxidation of malate to oxaloacetate by NAD*: malate + NAD+ → oxaloacetate + NADH + H+ In yeast mitochondria, where the pH = 8.1, this reaction is exergonic only at low oxaloacetate concentrations. Assuming a pH = 8.1, a temperature of 37 °C, and the steady-state concentrations given below, calculate the maximum concentration of oxaloacetate at which the reaction will still be exergonic. malate + NAD*→ oxaloacetate + NADH + H* lactate + NAD →→ pyruvate + NADH + H+ half reaction Pyruvate + 2H+ + 2e → lactate Pyruvate + CO₂ + H + 2e → malate Intracellular steady state concentrations: malate = 410 μM; NAD = 20.0 mM; pyruvate = 3.22 mM; NADH = 290 μM; AG=+29.7 kJ/mol AG¹ = +25.1 kJ/mol E° (V) - 0.190 - 0.330 lactate 1.1 mM CO₂ = 15.5 torr
- The glutamate dehydrogenase (GDH) catalyses the following reaction: *H3N- C H - CH₂ - CH₂ COO™ acide glutamique -COO + NAD+ + H₂O Time (min) A340 GDH COO™ с 5 1 2 3 4 1.760 1.718 1.675 1.635 1.595 CH₂ The answer: -1 - Vo 1.1.107 M.s-¹ - EA in 0.1 mL of GDH = 0.33 nkat CH₂ The activity of GDH is monitored in the sense of the formation of glutamate using the following conditions: 0.2 mL of 5 M ammonium sulphate 2.4 mL of buffer at pH 8 0.1 mL of NADH at 6.15 mg.mL-¹ (M = 709 g.mol-¹) 0.2 mL of 1 M a-ketoglutarate solution Warm mixture at 25 °C for 5 min Add 0.1 mL of GDH solution containing 1.6 mg.mL protein to start the reaction. COO CO acide a-cétoglutarique The change in absorbance at 340 nm is monitored, in a 1-cm cuvette, every minute for 10 min. Results are given in the table below: Data ENADH at 340 nm = 6220 M¹.cm¹ -1 + NH4+ NADH + H+ 6 1.550 7 8 10 9 1.510 1.489 1.476 1.451 Calculate the initial rate Vo of the reaction in M.s¹. - Calculate the enzyme activity of the volume of…Below is an image of the Krebs cycle: acetyl-CoA oxaloacetate COASH H20 NADH NAD* H20 malate citrate fumarate isocitrate FADH2 NAD* CO2 FAD АТР NADH + ADP succinate GTP NAD+ a-ketoglutarate H20 GDP NADH + CO2 COASH succinyl CoA COASH Consider the conversion of succinate to fumarate, which is coupled with the production the electron carrier FADH2. If this reaction was NOT coupled with the production of FADH2 (and only catalyzed the conversion of succinate to fumarate), how would this impact ATP production through cell respiration? OATP production would stop because no high energy electron carriers would be produced ATP production would still occur, but there would be a much lower ATP yield because a large number of electron carriers are no longer being made ATP production would stop because without FADH2 we will no longer have electrons moving through the electron transport chain ATP production would still occur, but there would be a slightly lower ATP yield because a small number of…Calculate and compare the AGº' values for the oxidation of succinate by NAD and FAD. Use the data given in the table to find the E' of the NAD: NADH and fumarate:succinate couples, and assume that E' for the enzyme-bound FAD : FADH₂ redox + couple is nearly +0.05 V. Oxidant NAD + Fumarate Reductant NADH + H Succinate + AGO for the oxidation of succinate by NAD AGO for the oxidation of succinate by FAD: n 2 E'o (V) -0.32 T -0.03 + FAD is an oxidant, whereas NAD is a reductant. + Why is FAD rather than NAD the electron acceptor in the reaction catalyzed by succinate dehydrogenase? + The oxidation of succinate by NAD is not thermodynamically feasible. + The oxidation of succinate requires two NAD molecules but only one FAD molecule. + The electron-transport chain can regenerate FAD, but not NAD˚. kJ mol-¹ -1 kJ mol-¹
- In relation to Carbamoyl Phosphate Synthetase enzyme, answer the following: A- What are the two isoforms of this enzyme, explain why there are two isoforms? B- What are the clinical manifestations associated with the deficiency of these two enzymes? C- Write down the biochemical reaction and the name of the metabolic pathway that these two isoforms are involved in, and how many ATP is utilized by these two isoforms?Compare the delta ΔG0' values for the oxidation of succinate by NAD+ and by FAD. Use the data given in Table 18.1 to find the E0' of the NAD+-NADH and fumarate-succinate couples, and assume that E0' for the FAD – FADH2 redox couple is nearly 0.05 V. Why is FAD rather than NAD+ the electron acceptor in the reaction catalyzed by succinate dehydrogenase?Chambers and coworkers have reported [NAD+] and [NADH] concentrations in yeast mitochondria as 20 mM and 0.3 mM, respectively. Consider the Malate Dehydrogenase reaction below: Malate + NAD+ → Oxaloacetate + NADH + H+ ∆G0’ = +29.7 kJ/mol If Malate concentration in yeast mitochondria is 0.4 mM what is the maximum concentration of oxaloacetate needed to make the reaction exergonic at pH 7.0 and 370C?