Not too sure if my answer is correct. For the reactionglutamate (aq) + oxaloacetate²- (aq)the equilibrium constant at standard temperature is Keg' = 2.82. What is the value ofeqAGO¹ for this reaction?Select one:6.99 kJ/mola-ketoglutarate²- (aq) + aspartate¯ (aq)-8.62 kJ/molO-2.57 kJ/mol-6.99 kJ/mol2.57 kJ/mol

Standards free energy change calculated at biochemical standards is called biochemical standard free…

Answered: For the reaction glutamate (aq) +…

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

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
Calculate AG for the reaction G+ H I + J when [G] = 0.0132 mM, [H] = 35.1 uM, [1] = 55.6 uM, [J] 18.7 uM, the temperature = 37 °C and AG°= -48.2 kJ/mol. Keep concentration units in uM. -50.3 kJ/mol -39.1 kJ/mol O-46 kJ/mol -25.8 kJ/mol
Triosephosphate isomerase catalyzes the conversion of glyceraldehyde 3-phosphate to dihydroxyacetone phosphate. This reaction has a Keq of 22.2. What is the standard free-energy change for this reaction? -7,680 kJ/mol -7.68 kJ/mol -3.34 kJ/mol -0.644 kJ/mol 7.68 kJ/mol
Calculate the Keq (report up to two decimal places and do not use scientific notation) for the net reaction at 298.15K. (see attached image) Note: R = 1.98 x 10 -3 kcal/mol-K
A 0.578-g saltwater sample was titrated with 1.864 g AgNO3 solution to reach the endpoint of the reaction. Calculate the following by showing all necessary solutions: 1. mol AGNO3 if the AGNO3 solution was prepared by dissolving 5.0 g of AgNO3 in distilled water until 100 ml is reached. (MW AgNO3 = 169.87 g/mol) 2. % Cl in the saltwater sample (MM CI = 35.45 g Cl /mol CI" )
Calculate ΔG for the reaction H2O(l) ⇆ H+(aq) + OH−(aq) at 25°C for the following conditions. [H+] = 3.1 M, [OH−] = 4.7 ×10−4 M
Assume that the reaction Arabinose +Pi Arabinose-6-P has a delta G of +16.1 kJ/mol and the reaction XTP XDP + Pi has a delta G of -24.7 kJ/mol. Calculate the delta G for the combined reaction Arabinose + XTP Arabinose-6-P + ADP, in kJ/mol to four significant figures.
At 298 K the standard enthalpy of combustion of sucrose is −5797 kJ mol−1 and the standard Gibbs energy of the reaction is −6333 kJ mol−1. Estimate the additional non-expansion work that may be obtained by raising the temperature to blood temperature, 37 °C.
Consider the following reaction at 25°C with the ΔG°’ = +1800 J/mol for the forward reaction.The molar concentrations at the beginning of the reaction were [A] = 19 mM and [B] = 10 mM.After 1 hour, the concentrations were [A] = 16 mM and [B] = 13 mM. Calculate the ΔG of the reaction at the 1 hour timepoint. Please round to 1 decimal point.Gas constant = 8.315 J/mol K
A monoprotic weak acid, HA, dissociates in water according to the reaction HA(aq) = H+ (aq) + A¯(aq) The equilibrium concentrations of the reactants and products are [HA] = 0.220 M, [H+] = 3.00 × 10−4 M, and [A¯] = 3.00 × 10−4 M. Calculate the value of pKa for the acid HA. pKa =
The formation constants at 25°C for Fe(CN)4-6 and Fe(EDTA)2– are 1.00 x 1037 and 2.10 x 1014, respectively. Answer the questions below. 1) Calculate K under standard conditions for the reaction Fe(EDTA)2−(aq) + 6CN−(aq) ----> Fe(CN)4−6(aq) + EDTA4−(aq) 2) Calculate ΔG° for the reaction. (kJ/mol)
The standard state free energy of hydrolysis of acetyl phosphate isΔG° = -42.3 kJ/mol. Acetyl-P + H2O acetate + Pi Calculate the free energy change for the acetyl phosphate hydrolysis in a solution of 2 mM acetate, 2 mM phosphate and 3 nM acetyl phosphate.

SEE MORE QUESTIONS

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

For the reaction glutamate (aq) + oxaloacetate²- (aq) a-ketoglutarate2- (aq) + aspartate¯ (aq) the equilibrium constant at standard temperature is Kea' = 2.82. What is the value of AGO¹ for this reaction? Select one: 6.99 kJ/mol -8.62 kJ/mol -2.57 kJ/mol -6.99 kJ/mol 2.57 kJ/mol