Consider the following chemical reaction 21CI(g) + H2(g) 2HCI +I (g) 2(s) Write the equation that relates the rate expressions for this reaction in terms of the disappearance of ICI and the formation 12.
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![Consider the following chemical
reaction
21CI(g) + H2(g)
2HCI +I
(g) 2(s)
Write the equation that relates the
rate expressions for this reaction in
terms of the disappearance of ICI
and the formation 12.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fd8a6ead5-1f7a-4a7e-8049-3111875dd153%2Fd209d168-3c8d-4c67-8f53-5463d146af3b%2Fxzcuj63_processed.jpeg&w=3840&q=75)
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- Utilising the provided class data generate the following graphs: I) Michaelis Menten; II) Lineweaver-Burk; and III) Hanes-Woolf. Ensure that you clearly label each graph,and add the relevant trendlines with equations. Table 1: Class data demonstrating the Absorbance at 700nm obtained for the alkaline phosphatase enzyme reaction Table 1 tube Abs700mm 1 0.000 2 0.060 2 0.090 4 0.140 5 0.190 6 0.250 7 0.290 The equipment we used are • 20mM Tris Buffer pH 8.5 • 33mM MgCl2 • Alkaline Phosphatase (2mg/ml) in 20mM Tris Buffer pH 8.5 • 4mM Glucose-1-phosphate • Acid Molybdate pH 5.0 • Reducing Agent • Distilled Water • Glass Test tubes • Tube Rack • Cuvette • Pipettes and Tips • Water bath set to 37oC The method we used is Method/Protocol: 1. Read the protocol in its entirety before starting. Take note of any additional information that appears in subsequent steps that may influence how previous steps are performed. 2. Using glass tubes, generate the reactions mixtures…Carbonic anhydrase catalyzes the hydration of CO. CO2 + H2O ¬ H½CO3 The Km of this enzyme for CO, is 1.20×104 µ.M. When [CO,] = 3.60×104 µM, the rate of reaction was 4.50 umol·mL! sec-1 a What is Vmax for this enzyme? umol·mL-!sec-!80mL of a 0.3M solution of hexapeptide Leu-His-Cys-Glu-Asn-Arg is adjusted to pH=pI. The solution is then titrated with 0.2M HCL to a final pH of 2.1. Sketch the titration curve, labelling the pH and volume axes. Indicate the volume of HCL needed to reach relevant pKa value and equivalence point(s)z Relevant pKa values are: 2.1, 4.3, 6.0, 8.3, 9.8, and 12.5.
- Quinine ( C20 H24 N2 O2) is the most important alkaloid derived from cinchona bark. It is used as an antimalarial drug. For quinine, pK, = 5.1 and pK, = 9.7 ( pKp = – log Kp). Only 1 g quinine will dissolve in 1920.0 mL of solution. Calculate the pH of a saturated aqueous solution of quinine. Consider only the reaction | Q+ H2O= QH+ + OH- described by pK, where Q = quinine. pH =In the electrolysis of aqueous sodium bromide, there are two possible anodic reactions: *2H2O(l) ——-> 02(g) + 4H+(aq) + 4e–, E° = 1.23V2Br–(aq) ——–> Br2(g) + 2e-2, E° = 1.08 VWhich reaction occurs at anode and why?For a Michaelis-Menten reaction, k₁=5 x 107/M-s, k-1-2 x 104/s, and k2=4 x 10²/s. Calculate the Ks and KM for this reaction. Does substrate binding achieve equilibrium or steady state?
- The equation of the double reciprocal plot is y = 0.5294 x + 1.4960. What is the value of vmax (in M/s)? The substrate concentration is given in units of molarity (M) and reaction velocity has units of molarity per second (M/s). (Report to three significant figures)ver is given. A +B C+ D 1) Calculate AG for the above react un and indicáte whether the reaction is favorable or unfavorable [A] = 0.9 M 20°C AG° = 4 KJ/mol %3D [B] = 15mM [C] = 4mM [D] = 3 M R= 8.314 J/moleK %3D %3D 4.7 and explain how you know.80mL of a 0.3M solution of hexapeptide Leu-His-Cys-Glu-Asn-Arg is adjusted to pH=pl. The solution is then titrated with 0.2M HCI to a final pH of 2.1. Sketch the titration curve, labelling the pH and volume axes. Indicate the volume of HCl needed to reach each relevant pKa value and equivalence point(s). Relevant pka values are: 2.1, 4.3, 6.0, 8.3, 9.8, and 12.5.
- Aerobic degradation of an organic compound by mixed cultureof organism in wastewater can be represented by following reaction. C3H6O3 + a O2 + b NH3 → c C5H7NO2 + d H2o + e CO2 A. Determine a, b, c, d and e, if YX/S = 0.4 d X/g S. B. Determine the yield coefficients YX/O2 and YX/NH3. C. Determine the degree of reductions for the substrate, bacteria and RQ for the organismsIf we were handed a tuke of 2mg/mL BSA how much is required 20μL of each of the following Concentrations? to make zoul total bring up to volume with dH ₂0 @ 01125 mg/mL (1) 0,150 mg Ⓒ 0.50 mg/mL @ 0.75 mg/mL Ⓒ 1.0mg/ml /ML Can it be solved using C₂ C₁V₁ = C₂ V₂ If CI= V₁ yes, please show work. VzChitinase is a protein that breaks down chitin, a primary component of the cell wall in fungi, scales in fish and exoskeletons of arthropods. The activity of chitinase extracted from a plant was shown to be optimum at pH 5. You were tasked to prepare 300 mL of 150 mM buffer solution for further analysis of the extracted chitinase. REAGENTS Ka 2.5M Acetic acid Solid NaOAc•3H2O [136.08g/mol] 1.76 x 10-5 2.5M NH3 Solid NH4Cl [53.49g/mol] 5.6 x 10-10 2.5M Lactic acid Solid sodium lactate [112.06g/mol] 4.0 x 10-5 5 M HCl 5M NaOH Pls show sol'ns 1. Given the following reagents, give the moles of each component (acid & base).2. What are the mass/volume of the components needed to prepare the buffer? 3. What will the pH of the buffer be if 1mL of 5 M NaOH was added?