which are true The standard reduction potential for (NAD*/NADH) is -0.320 V and the standard reduction potential for (Pyruvate/Lactate) is -0.185V. Which of the following statements are True?O Multiple answers: Multiple answers are accepted for this questionSelect one or more answers and submit. For keyboard navigation. SHOW MORE VAE,' for the reaction = -0.135 VaThe standard reduction potential indicates the electrons will flow from NADH to PyruvateThe standard reduction potential indicates the electrons will flow from Lactate to NAD*The Ken for the reaction is 36800If [Pyruvate] = 0.05 mM and [Lactate] = 2.9 mM and AG for the Lactate Dehydrogenase = 15 kJ/mole in erythrocytes the[NAD+]/[NADH] ratio under these conditions is 1.48ehe complete reduction of one molecule of 02 gas requires two electronsIn the Q Cycle two protons are pumped into the matrixNADH is a two-electron donoriUQH, donates electrons to Complex III

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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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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). 11/12102 + 2H* + 2e¯ → H₂0 NAD + H* + 2e → NADH O-1.136 volts 0.496 volts +1.136 volts -0.496 volts EU (volts) – 0.320
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
Your current Vmax (4x10-3 A/S) from the Michaelis-Menten plot has the units of A/s and was determined using 0.1 mg of ADH in a total volume of 1.25 mL. Use the Beer-Lambert equation followed by simple conversion to express your estimated Vmax in (mol )/s per 1 mg ADH. The molar absorptivity of NADH at 340 nm is 6220 L/(mol*cm).
Perform the calculations to make a master mix for 20 1.0 mL reactions each composed of 165 uL of 6 mM NAD+ 165 uL of 0.15M Lactate and 630 uL of 0.15M CAPS pH 10.5 per reaction. Report your answers in units of milliliters.
You make reaction progress curve by plotting absorbance vs time (seconds) and find the equation of the line to be y = -0.00235x + 0.7129. Calculate the U/µL and U/mL of lactate dehydrogenase activity in this fraction. The LDH activity is done identical to what is indicated in the lab manual. Show each step of the calculation from AU/time to M/min, to mol/min, to µmol/min to µmol/min/µL (=U/µL).
The standard reduction potential for ubiquione (A or coenzyme Q) is .045 V, and the standard reduciton potential (E) for FAD is -0.219 V. Using these values, show that the oxidation for FADH2 by ubiquinone theoretically liberates enough energy to drive the synthesis of ATP. Faraday constant =96.48KJ/Vol delta G' standard for ATP Synthesis is +30.5 KJ/mol R=8.314 J/mol K=1.987 cal/mol K
Use the Michaelis-Menten equation to complete the enzyme kinetic data set, when Km is known to have a value of 1 mmol/L. Upload your tabulated answers and show your calculations.
a) Calculate the enzyme and specific activity of a reaction with 3 pM Hsp90 using the following information: The rate is measured in a spectrophotometer as 0.028 OD units/min in a 1 ml reaction volume. The absorbance was detected at 340nm and the extinction coefficient for NADH at this wavelength is 6200L M- 1 min-1 and the molecular mass of Hsp90 is 82.7 kDa. The rate of NADH utilisation is equivalent to the rate of ATP utilised by Hsp90. Show all your calculations and the units for your answers. b) Calculate the turnover number for the reaction described in (a) above
Begining with 1 M concentrations of each reactant and product at pH=7 and 25.0 degrees C, calculate the K'eq of the reaction Pyruvate + NADH Lactate + NADH+H+. Note the temperature of this reaction will not affect the standard reducton potential delta E° in the table 13-7b.
Proline racemase catalyzes the conversion between L-proline and D-proline. The Km and kcat for this reaction are 0.15 M and 550/sec respectively. If the enzyme concentration is 1.45 X 10-5 mmole/ml what is the Vmax of this reaction?
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-!
Hexokinase in red blood cells has a Km of approximately 50 µM. What concentration of blood glucose would yield a velocity equal to 90 % Vmax? Select an answer and submit. For keyboard navigation, use the up/down arrow keys to select an answer. a 500 mM 0.0450 mM 4500 μΜ 5000 µM e 5.0 mM 0.50 mM 450 μΜ 4.5 mM 50 μΜ.

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