Standard redox potentials Eo' for some common compounds in biochemistry:Eo' (Volt)+ 0,81+0,42+ 0,2512 O₂ + 2 H+ + 2 eNO3 + 2 H+ + 2 e2 cyt c (ox) + 2 e2 cyt b (ox) + 2 ePyruvate + 2 H+ + 2 e*NAD + 2 H+ + 2 eAcétoacétate + 2 H+ + 2 e(2) acétoacétate + NADH + H+H₂ONO₂ + H₂O2 cyt c (red)2 cyt b (red)Lactate(3) 2 cyt c (ox) + 2 cyt b (red)NADH + H+B-hydroxybutyrate+ 0,08- 0,19With the help of the above table, determine the spontaneous direction of the followingreactions in the standard conditions. Justify your answers by calculating the Gibbs(free) energy of reaction in each case.(1) pyruvate + ß-hydroxybutyrate-0,32- 0,35lactate + acétoacétateB-hydroxybutyrate + NAD+2 cyt c (red) + 2 cyt b (ox)

If the Gibbs free is negative for a reaction then the process is said to be spontaneous. A positive…

Answered: Standard redox potentials E' for some…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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In considering active transport by Na + -K + -ATPase at body temperature (37 o C), 3 Na+ are pumped out of the cell and 2 K + are pumped in for each ATP that is hydrolyzed to ADP + P i . Given that underyour experimental conditions, the DG for ATP hydrolysis is -10 kcal/mol, and that V is -60 mV, and that the pump maintains the internal Na + at 10mM, external Na + at 120 mM, internal K + at 120 mM and external K + at 8mM, what is the efficiency of the pump (i.e., what fraction of the energy available from ATP hydrolysis is required to drive transport at the provided levels)?
Write out the full redox reaction that happens when both of these reactions are added to the same reaction where there is 1M concentrations of each reactant and products, pH7, and temeprature is 290K. Identify which compounds will be reduced and which compounds will be oxidized. redox reaction 1: Pyruvate¯ + 2H+ + 2e¯ → lactate¯ E'o(V) = -0.185 redox reaction 2: NAD+ + H+ + 2e¯ → NADH E'o(V) = -0.320
Calculate AG for the below balanced redox reaction as written. You may find a list of standard reduction potentials useful. 3 12 (s) + 2 Al (s) → 61 (aq) + 2 Al3+ (aq) O-4.24 x 102 kJ/mol O-6.48 x 102 kJ/mol O -2.12 x 102 kJ/mol O-1.27 x 103 kJ/mol O-6.37 x 102 kJ/mol
Please provide an explanation for how to work through this practice problem: Using table 12.1, calculate the free energy change for the synthesis of ATP from cAMP and inorganic phosphate. (Note: cAMP is hydolyzed to AMP, and the free engery of hydrolysis for ATP and ADP is approximately equal.) Table 12.1: (Compound: Change in Free Energy in kJ/mol) cAMP: -50.4 Creatine phosphate: -43.3 ATP: -30.5 Glucose 6-phosphate: -13.9 AMP: -9.2
The hexapeptide Ala-Met-Leu-Lys-Phe-Asp is digested in the same tube with both Cyanogen Bromide and Trypsin at the same time at pH=7. Draw the structure of the product(s) that would bind to a cation exchange column. (Relevant pKa values are 2.2, 3.9, 9.5 and 10.5. Assume pKa values for any newly generated a-amino and a-carboxyl groups are 9.5 and 2.2 respectively)
make a schematic diagram of BChE/AChE inhibitory determination Butyrylthiocholine iodide (BChI), as well as acetylthiocholine iodide(AChI) molecules were utilized as substrate compounds of the reaction. Inthis regard, 5,5′‐dithio‐bis(2‐nitro‐benzoic acid) compound (DTNB) wasused to estimate BChE/AChE activity. In summary, 100 μL Tris buffersolution (HCl, 1.0M, pH 8.0, Tris) and variety of concentrations of thesample solution (50‐200 mL) were added in deionized water and also20 μL of BChE/AChE enzymes solutions added. The mixture was thenincubated for 10 minutes at 20°C. Finally, 50 μL of DTNB (0.5 mM and25 mL) BChI/AChI were added to the incubator mixture. The reactionwas also started by adding 50 μL BChI/AChI. The activity of theseenzymes was evaluated using spectrophotometric spectra with awavelength of 412 nm.
(b) the activity of the malate-aspartate shuttle (MAS) system of isolated rat brain mitochondria suspended in an isotonic me- dium buffered to pH 7.4. Diagram A illustrates NADH fluo- rescence emission upon addition of Glutamate in the ab- sence and presence of Aspartate. Diagram B illustrates sim- ilarly NADH fluorescence emission upon addition of Gluta- mate in the presence of Aspartate followed by additions of submicromolar concentrations of Ca2+. As is well estab- lished, the MAS in brain, skeletal muscle, and cardiac mus- Diagrams A and B on the right show changes in Glu A Glu В -No Asp + 0 +0.12 -0.48 + 16 0.81 +1.8 ++ Asp 10 min 2 min cle mitochondria is activated by cytosolic concentrations of Ca2* < 3 µM. To simulate the cytosolic part of the MAS, the following reagents were added to the medium: 4 units/ml glutamate-oxaloacetate transaminase, 6 units/ml malate dehydrogenase, 66 µM NADH, 5 mM aspartate, 5 mM malate, 0.5 mM ADP, 200 nM ruthenium red (to block the mitochondrial…
The standard Gibbs (free) energy of reaction (A,Gº') of the following reaction is equal to zero (at 25 °C and pH 7) pyruvate + aspartate Pyruvate, aspartate and L-alanine are mixed each at a concentration of 1 mM, without oxaloacetate. Calculate the molar concentrations of each compound when the reaction reaches equilibrium. oxaloacétate + L-alanine
Chymotrypsin has the highest affinity for which of the following substrates: Table. The values of KM and kcat for some Enzymes and Substrates Enzyme Chymotrypsin Ки (М) 4.4 x 10-1 8.8 x 10-2 6.6 x 104 Kcat (S-1) 5.1 x 10-2 1.7 x 10-1 1.9 x 102 Substrate N-acetylglycine ethyl ester N-acetylvaline ethyl ester N-acetyltyrosine ethyl ester Catalase H2O2 2.5 x 10-2 1.0 x 107 Urease Urea 2.5 x 10-2 4.0 x 105 OA. N-acetylglycine ethyl ester OB. N-acetylvaline ethyl ester OC. N-acetyltyrosine ethyl ester D. Urea
NOTE: the enzyme-inhibitor complex requires 450 joule/mol to dissociateJOULE/MOL
Many years later, in 1989, Wild, et al. revisited the idea of allosteric control of ATCase by CTP. They noted that CTP did indeed inhibit ATCase, but that the inhibition was always incomplete, even at high concentrations of CTP. They hypothesized that perhaps CTP did not act alone, but in combination with some other nucleotide. They tested the activity of ATCase in the presence of several nucleotide combinations. The results are shown in Table 3. a. What combination gives the most effective inhibition? b. What is the physiological significance of this combination? c. Revise Figure 1 to include this new information. d. Redraw Figure 2 to include this new information. How does the combination compare with the values for the nucleotides alone? Table 3: Relative specific activities for combinations of nucleotide effectors. A value greater than one indicates stimulation, a value less than one indicates inhibition. Nucleotide Effector ATP CTP GTP UTP ATP/CTP ATP/GTP ATP/UTP CTP/GTP CTP/UTP…
By what factor is sample A2 more concentrated than sample A1?

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