Consider the following redox reaction:lactate + NAD = pyruvate + NADH + H+The relevant reductive half reactions are as follows:pyruvate + 2e + 2H+ lactateNAD+ + 2e+ H* = NADHE' -0.185 V=E' -0.320 VWhat is the AE' of the redox reaction?-0.505 V-0.135 V0.135 V○ 0.505 V

Step 1: Δ'Eo (standard cell potential) is the measure of the potential difference between two half…

Answered: Consider the following redox reaction:…

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

See similar textbooks

Similar questions

All dehydrogenases of glycolysis and the TCA cycle use NAD* (E° for NAD*/NADH is -0.32V) as electron acceptor except succinate dehydrogenase (which uses FAD (E° for FAD/FADH2 is 0.05V). Based on AG° = -NFEº, show and state (1-2 sentences) why is FAD a more appropriate electron acceptor than NAD* in the dehydrogenation of succinate (consider the E° values of %3D Uptake in Na+ Vmax Uptake in absence of Na+ Vmax substrate K: (mM) Kt (mM) L-leucine 420 0.24 23 0.2 D-Leucine 310 4.7 5 4.7 L-valine 225 0.31 19 0.31 fumarate/succinate (E° = 0.031), NAD*/NADH, and the succinate dehydrogenase FAD/FADH2).
This is a picture of the catalysis of alcohol by ADH with an inhibitor binding as an aldehyde analog. I have two questions. First, what would the enzyme be classified as and why? Also, what would the steps of this mechanism be?
Certain bacteria can respire in anoxic environments using arsenic (V) as electron acceptor. The relevant unbalance half reactions are: H₂ AsO+H → H¸AsO +H₂O, logK = 10.84, AG = -14.5kca I m I ol-e CH₂O+H₂OH + CO2 (g), logK = 1.2, AG° = -1.63kca — ol-e 1) Balance the two half reactions 2) What is m the overall respiration reaction, standard free energy change \Delta GO 3) Is this process energetically more or less favorable than sulfate reduction? (\Delta GO for the reduction of sulfate to HS- is -5.78 kcal/mol - e-) 4) If [H2AsO4-] = [ H3ASO3] = 0.5 mM and pH = 7, estimate pe of the system
What is the reaction potential for oxidation of NADH (for completely passing electrons from NADH to O2) with units? 2. What is the reaction potential for oxidation of FADH2 (from FADH2 to O2) with units? 3. Which reaction has a more negative deltaG?
Which of the following statements are False?
Consider the reaction: malate + NAD+ → oxaloacetate + NADH + H+. Calculate ΔE°’ for the reaction.
Provide a reasonable step-wise mechanism for the reaction below, involving TPP as acoenzyme (can abbreviate the pyrophosphate as R), and invoking any general acids or base fromacetolactate synthase that you might need .
Table 1 shows the kinetic data that have been obtained for glucoamylase from Aspergillus niger at different temperatures in the production of glucose from maltodextrin. The rates of reaction measured are using an enzymes concentration of 0.003 μmolml-¹. Table 1: Glucoamylase Activity at different temperatures Maltodextrin Concentration (μmol/L) 0.5 1 1.5 2.2 5.5 11 Initial Reaction Velocity (μmol/L.s) T = 40°C 2.1 3.5 4.9 5.6 589 8.3 9.3 T = 60°C 5.2 9.7 13 16 23 31
Consider the malate dehydrogenase reaction from the citric acid cycle. Given the listed concentrations, calculate the free energy change for this reaction at energy change for this reaction at 37.0 °C (310 K). AG' for the reaction is +29.7 kJ/mol. Assume that the reaction occurs at pH 7. [malate] 1.25 mM [oxaloacetate] = 0.290 mM [NAD+] = 430 mM [NADH] : = 170 mM AG : kJ-mol-1 * TOOLS x10
i) Re-arrange the Michaelis Menten equation so it involves the ratio [S]. Show all steps beginning Km noting any assumptions or required conditions. Km ii) Calculate the ratio [lo for the case when the rate of product formation is 68% of Vmax and the substrate is in great excess. d[P] dt : k₂ with = [E],[S] Km+[S]' [S]o Km iii) Explain, in a few sentences, why the ratio determines the ratio V Vmax V Vmax Begin by explaining the meaning of stating simply "it's the ratio...." is not sufficient. Include in your explanation the factors that effect v and Vmax. Consider what factors make v different from or equal to Vmax. Consider what Km represents concerning processes involving ES. " iv) Calculate KM at 310K at given the following rate constant information: k₁ = 17 s-¹M-1 at 300K with A = 7300 s-¹M-1 K-1₁ 6 s¹ at 300K with A = 14500 s -1 k₂ = 31 s¹ at 300K with A = 600 s-¹
Please answer both parts, i and ii
Glyceraldehyde-3-phosphate (GAP) is converted to 1,3-bisphosphoglycerate (1,3-BPG) as shown. GAP + P + NAD+ 1,3-BPG + NADH Is this reaction spontaneous? How do you know? AG = 6.7 kJ mol-¹ The reaction shown above is coupled to the following reaction in which 1,3-BPG is converted to 3-phosphoglycerate (3-PG): GAP + P + NAD+ + ADP3-PG + NADH + ATP AG = -18.8 kJ mol-¹ 1,3-BPG+ADP3-PG+ATP Write the equation for the overall conversion of GAP to 3PG. Is the coupled reaction favorable? How do you know?

Recommended textbooks for you

Biochemistry

ISBN:

9781319114671

Author:

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

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781319114671

Author:

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

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781305961135

Author:

Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Fundamentals of General, Organic, and Biological …

Biochemistry

ISBN:

9780134015187

Author:

John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson

Publisher:

PEARSON

SEE MORE TEXTBOOKS

Consider the following redox reaction: lactate + NAD = pyruvate + NADH + H+ The relevant reductive half reactions are as follows: pyruvate + 2e + 2H+ lactate NAD+ + 2e+ H* = NADH E' -0.185 V = E' -0.320 V What is the AE' of the redox reaction? -0.505 V -0.135 V 0.135 V ○ 0.505 V