Can you please explain the relationship of ATP concentration and NADH concentration in this graph (cellular respiration)? At different treatments of ATP (E.g. At 25 ATP, 50 ATP, 100 ATP), why did the NADH concentration change?
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Can you please explain the relationship of ATP concentration and NADH concentration in this graph (
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- Substrate Initial velocity Vo concentration [S] µM s-1 10 0.13 25 0.27 50 0.45 100 0.65 150 0.77 200 0.85 300 0.94 500 1.03 1. Calculate Vmax and Km??? The enzyme is dissolved at a concentration of 1 mg/ml and has a molecular weight of 50 kDa. a) What is the turnover number of the enzyme? b) What is the specificity constant of the enzyme? c) Is the enzyme operating near the maximum rate possible, i.e. is the enzyme diffusion controlled? please show all working and formulas as I am trying to learn. thank youDiscuss two approaches (methods) based on week-intermolecular forces on detection of ATP over AMP? please explain, hand written answer will be preffered, thanksA solution containing 0.00001 M ATP has transmission 70.2\% at 260 nm in 1 cm cuvette calculate the transmission of solution in a 3 cm cuvette
- Calculate the ΔG° for the making of 30 ATP from 30 ADP ATP + H2O ↔ ADP + Pi ∆G°’ = –30.5 kJ/mol ATP + H2O ↔ AMP + PPi ∆G°’ = –45.6 kJ/molQuestion: Determine the Km and Vmax for this enzyme/substrate combination. [Substrate] (mM) V0 (mM/min) 0.25 0.183 0.50 0.356 1.00 0.665 2.50 1.45 5.00 2.35 What is the concentration of substrate necessary to achieve a turnover rate of 1.00 mM/min?The pH values of the different compartments are shown below: matrix Intermembrane space Cytosol pH 7.8 – 8.0 pH ~ 7.0pH 7.0 – 7.4 Proton flow through ATP synthase leads to the formation of ATP, a process defined as the binding-change mechanism that was initially proposed by Boyer. Briefly explain Boyer’s binding change mechanism for the ATP synthase.
- YA *H 23. Write free energy change (AG), standard free energy change (AG), and biochemical free energy change conditions (AG") (leave blank if something doesn't apply to the condition) Temperature Pressure Reactant's initial conc. [H+] conc. [H₂O] Free energy change standard free energy (AG) change (AG") Biochemical standard free energy change (AGI)Matching Question: Researchers characterized a new enzyme and determined its Km=200 uM. Moreover, they found that at (Etotad10 nM this enzyme reaches maximum reaction velocity Venasa5 is 1. What is the keat of this enzyme? 2. At which concentration of the substrate this enzyme reaches initial reaction velocity (Vo) of 500 nM/s (assuming (Etotal is the same 10 nMy? 3. What is the maximum reaction velocity (Vmax) of the reaction catalyzed by this enzyme at (Etotail4 nM? Make sure to choose the correct units of measure. Note that some of the items from the answer list should NOT be used. v kcat 1. 400 uM - (S] - - Vmax 2 100 uM 500 s 450 uM 250 s1 * 501 7. so00 s 1 UM's SuMis 10 200 uM 11. 10 uMis 12 25 s 13. 500 nM/sNational Board of Medical Examiners Biochemistry Mark 36. In the presence of a metabolite (X), 6-phosphofructokinase is assayed at a fixed concentration of ATP and varying concentrations of fructose 6-phosphate. The resulting data are shown in the table. Fructose 6-phosphate (pM) 5 10 20 40 75 100 200 Velocity umoles/min 0.05 0.15 0.25 0.70 1.7 2.2 3.1 3.1 Velocity (+X) umoles/min 0.006 0.025 0. 10 0.35 1.03 16 2.9 3.1 400 Metabolite (X) is most likely which of the following substances? O A) ADP O B) AMP OC) CAMP D) Citric acid O E) Fructose-2,6-bisphosphate
- What is the Vmax of an enzyme at 1 μM with -4G RT k = 6.2x 10¹2 s-1 (Ideal gas constant R = 8.314 J K-1 mol-1) cat 0.14 μM S-1 1.4 µM s-1 14 μM s-1 0.14 mM s-1 1.4 mM s-1 activation energy (AG) of 55000 J/mol at 298K?CALCULATIONS OF THE SOLUTIONS FOR EXPERIMENT Substrates Stock concentations Succinate + glutamatate (G/S) 150 mM Glutamtate + 150 mM Succinate Malate + pyruvate (M/P) 30 mM Malate + 30 mM Pyruvate Inhibitors Substrates of ETC ATP stock (50 µM): Make pre-dilutions with 20, 15, 10, 5, 2,5 and 1,25 μM ATP (1000 μL of each) Rotenone Oligomycin CCCP KCN Antimycin A Calculate the needed volumen of the standards! Inhibitors of ETC Stock concentations 400 µg/ml in DMSO 1250 µg/ml in EtOH 1000 µg/ml in DMSO 400 mM in Tris-buffer 1 mg/ml in DMSO Calculate the needed volumen! Final concentrations (in 250 μL) 8 μg/ml 25 µg/ml 20 µg/ml 8 mM 20 µg/mlQ 09 (7.5 pts.): Problem: 1.00 nM of enzyme (E), when allowed to react with 30.0 µM substrate (S), has a measured initial velocity of 3.00E2 nM/s. What is the Km for this ES reaction if the kcat is 4.00E2 s-1?