Malate dehydrogenase catalyzes the oxidation of malate to oxaloacetate with a standard Gibbs free energy of AG° +29.7 What is the equilibrium constant (Keq) for this = mol reaction at 298 K and pH 7? Under physiological conditions at 310 K and pH 7, this reaction is at equilibrium. In the mitochondrial matrix, the ratio NAD+/NADH is 8 and the concentration of malate is 1.0 mM. What is the concentration of oxaloacetate? Malate dehydrogenase is also present in the cytoplasm where the ratio NAD+/NADH is 700 and malate concentration is 1.0 mM. If this reaction is at equilibrium at 310 K and pH 7, what is the cytosolic concentration of oxaloacetate? malate + NAD+ oxaloacetate + NADH + H+

Assume that in a certain cell, the ratio of products/reactants or Keq = 747.1 (Keq is dimensionless) for the reaction Glucose + ATP <> Glucose-6-P + ADP, at a particular instant, the concentrations of each compound were Glucose =2.0M, ATP =7.7M, ADP =10.2M and G-6-P =21.5M. Calculate the difference (dimensionless) between Keq and the ratio of products/ractants at this instance, in this cell, to five significant figures.

What is the standard free energy (∆G0’) for the reduction of coenzyme Q by NADH as carried out by Complex I (NADH-CoQ Reductase) of the electron transport pathway if E0’(NAD+/NADH) =-0.10 V and E0’ (CoQ/CoQH2) = +0.095 V. Answer Choices

3) Calculate the physiological AG for the reaction: Phosphocreatine + ADP - creatine + ATP at 25 °C as it occurs in the cytosol of neurons, in which phosphocreatine is present at 4.7 mM, creatine at 1.0 mM, ADP at 0.20 mM, and ATP at 2.6 mM, knowing that Phosphocreatine + H20 - creatine + Pi AG° = -43 kJ/mol and ATP + H20 ADP + Pi AG = -30.5 kJ/mol

When the terminal phosphate is cleaved from the ADP molecule, the products are adenosine diphosphate and inorganic phosphate: ATP + H2O  ––>  ADP  +  Pi where Pi stands for the various forms of phosphate that exist at the pH of the particular solution.  If the total concentration of Pi  is 2.5 x 10–2 M, what are the concentrations of the predominant forms of phosphate that exist at pH 7.4?

2. Experimental Determination of Keq' and AG If a 0.1 M solution of glucose 1-phosphate at 25 °C is incubated with a catalytic amount of phosphoglucomutase, the glucose 1-phosphate is transformed to glucose 6-phosphate. At equilibrium, the concentrations of the reaction components are Glucose1-phosphate glucose6-phosphate 9.6 x 10-2 M 4.5 x 10-3 M Calculate Keg' and AG for this reaction.

年一年 phosphoglycerate mutase (PGM) H-C-OPO; H-- OH H-S-OPO; H-C- OH H H 3-Phosphoglycerate (3PG) 2-Phosphoglycerate (2PG) Does the oxidation number change for the carbon atom to which the phosphate is attached? (i.e., does C3 in 3PG have a different oxidation number than C2 in 2PG?) If so, does it become higher or lower? Oxidation number decreases when the phosphate is moved from C3 to C2. Carbon 3 has an oxidation number of 0; carbon 2 has an ox. number of +1. There is no change in the oxidation number, both atoms have oxidation number of -1. Oxidation number increases when the phosphate is moved from C3 to C2. Carbon 3 has an oxidation number of 0; carbon 2 has an ox. number of +1. Oxidation number decreases when the phosphate is moved from C3 to C2. Carbon 3 has an oxidation number of -1; carbon 2 has an ox. number of 0. There is no change in the oxidation number, both atoms have oxidation number of 0. O Oxidation number increases when the phosphate is moved from C3 to C2. Carbon 3…

Calculate the equilibrium constant at 37oC for the reactionGlucose + 6O2 + 36ADP + 36Phospate → 6CO2+ 42H2O +36ATP ... ... ...Entropy change of Go= − 423 kcal/mole of Glucose

Glycerol-3-phosphatase catalyzes the hydrolysis of glycerol-3-phosphate according to the following reaction.Glycerol-3-P + H₂O ⇌ glycerol + Pi When the enzyme is added to a solution of 1.25 M glycerol-3-phosphate at 25.0°C, and the reaction proceeds to equilibrium, the equilibrium concentration of glycerol-3-phosphate is 3.60×10⁻² M. Calculate the standard free energy of hydrolysis of glycerol-3-phosphate.

Intracellular concentrations in resting muscle are as follows: fructose- 6-phosphate, 1.0 mM; fructose-1,6-bisphosphate, 10 mM; AMP, 0.1 mM; ADP, 0.5 mM; ATP, 5 mM; and Pi, 10 mM. Is the phosphofructokinase reaction in muscle more or less exergonic than under standard conditions? By how much?