Please show all your work please, thank you! Sorry, this question has many parts. The reaction O3(g)+O(g)→2O2(g), occurs via the following mechanism: Step 1: Cl(g)+ O3(g)→ClO(g)+O2(g); Ea=85 kJ/mol Step 2: ClO(g)+ O(g)⇌Cl(g)+O2(g); Ea=10 kJ/mol a. Given the proposed mechanism above, identify any catalysts and any intermediates in this reaction. Be sure to distinguish between the two types of species in your answer. b. Using the proposed mechanism, derive a rate law. *Hint: use the activation energies to determine the slower step. Show all of your work. c. This mechanism was verified by kinetic measurements of the rate of depletion of ozone. How is the rate of change of oxygen gas concentration related to the rate of change of ozone concentration

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Refer to the figure shown here, and determine the value of E for the overall oxidation/reduction reaction (refer to the book/lecture slides if you need help with the overall reaction). 121/202 + 2H+ + 2e → H₂0 NAD + H* + 2e → NADH O-1.136 volts O 0.496 volts O+1.136 volts voltsm -0.496 volts EU (volts) +0.816 - 0.320

Determine whether the following reactions will be spontaneous under standard biochemical conditions. Include calculations for Delta G in your answer. Use Table 13-7 in your textbook to help you.a) 2NADH + 2H+ + O2 --> 2NAD+ + 2H2Ob) Malate + FAD --> Oxaloacetate + FADH2c) Pyruvate + H2S --> Lactate + S

Could you help propose a reasonable mechanism for the following biochemical transformation?

The enzyme enolase has a permanently bound Mg2+ ion in its active site. To the below is a schematic of the enzyme active site bound to an intermediate of the reaction. Which of the following are true? (Pick two.) PO32- Н Mg2 C C H HO Favorable electrostatic interactions (dashed blue lines) between Mg2+ and the intermediate increase (make it more positive) the AG of the reaction. Favorable electrostatic interactions (dashed blue lines) between Mg2+ and the intermediate decrease (make it more negative) the AG of the reaction. Favorable electrostatic interactions between Mg2+ and the intermediate decrease the rate constant, k, of the reaction, decreasing the rate of the reaction. Favorable electrostatic interactions between Mg2+ and the intermediate increase the rate constant, k, of the reaction, increasing the rate of the reaction.

Which of the compounds shown below exhibit a high negative free energy of hydrolysis equal to or larger than the free energy of hydrolysis for the phosphoanhydride of ATP? (Choose all that apply) В Α HPΗ Ho HO HO H2N-CH-C CH2 H2N-CH-C CH2 CH2 H2N-CH-Ö CH2 C CH2 D E O A O B O E O=p-00 O=p-00 O=-00 O=0-00 O=L-00

Convert the following reactions into "Metabolic Engineering" notation: C6H1206 + 2 H20 → 2 C2H60 + 2 HCO3 + 2 H* b. ATP + glucose > glucose-6-phosphate + ADP 3.

The following question focuses on how the parameters regulating enzyme function might change, and how these might appear graphically on a Michaelis-Menten plot and a Lineweaver-Burke plot. Carbonic anhydrase is an enzyme that will convert CO2 and water into HCO3. CO2 + H20 > H+ + HCO3 There are many different isoforms of this enzyme. (see for instance http://en.wikipedia.org/wiki/Carbonic_anhydrase 1 Assume that one variant has a Km of 10 µM and a different variant has a Km of 100 µM. Draw on the same graph a typical Michaelis-Menton plot showing the alteration in the rate of carbonic anhydrase as the CO2 level is varied for the two different variants of enzyme, assuming the concentration of the enzyme (10 mM) in the test tube is kept constant. Assume that you have equal amounts of the two different variants of carbonic anhydrase in a number of test tubes and that the Vmax for both enzymes are the same. Be sure to label the axes. For the same conditions as above, draw a…

3. 1,3-bisphosphglycerate has a high energy bond that can be used to phosphorylate ADP to make ATP according to the equation below. The free energy of hydrolysis of 1,3- bisphophoglycerate and ATP under standard conditions are -49.4 kJ/mol and -30.5 kJ/mol, respectively. If the [ATP] to [ADP] is about 4 in the cell, how much 1,3-bisphophoglycerate is needed relative to 3-phosphoglycerate to keep this formation of ATP spontaneous? -203PO. H- -OH -OPO3-² + ADP H- -OH -OPO3-² + ATP