If the ∆G'° of the reaction A -> B is –40 kJ/mol, under standard conditions the reaction:

When a mixture of 3-phosphoglycerate and 2-phosphoglycerate is incubated at 25 °C with phosphoglycerate mutase until equilibrium is reached, the final mixture contains six times as much 2-phosphoglycerate as 3-phosphoglycerate. Which one of the following statements is most nearly correct, when applied to the reaction as written? (R = 8.315 J/mol·K; T = 298 K) 3-Phosphoglycerate -> 2-phosphoglycerate

When a mixture of glucose 6-phosphate and fructose 6-phosphate is incubated with the enzyme phosphohexose isomerase (which catalyzes the interconversion of these two compounds) until equilibrium is reached, the final mixture contains twice as much glucose 6-phosphate as fructose 6-phosphate. Which one of the following statements is best applied to this reaction outlined below? (R = 8.315 J/mol·K; T = 298 K) Glucose 6-phosphate -> fructose 6-phosphate

Hydrolysis of 1 M glucose 6-phosphate catalyzed by glucose 6-phosphatase is 99% complete at equilibrium (i.e., only 1% of the substrate remains). Which of the following statements is most nearly correct? (R = 8.315 J/mol·K; T = 298 K)

The reaction A + B -> C has a ∆G'° of –20 kJ/mol at 25° C. Starting under standard conditions, one can predict that:

For the following reaction, ∆G'° = +29.7 kJ/mol. L-Malate + NAD+ -> oxaloacetate + NADH The reaction as written:

During glycolysis, glucose 1-phosphate is converted to fructose 6-phosphate in two successive reactions: Glucose 1-phosphate -> glucose 6-phosphate ∆G'° = –7.1 kJ/mol Glucose 6-phosphate -> fructose 6-phosphate ∆G'° = +1.7 kJ/mol ∆G'° for the overall reaction is:

The standard free-energy changes for the reactions below are given. Phosphocreatine -> creatine + Pi ∆G'° = –43.0 kJ/mol ATP -> ADP + Pi ∆G'° = –30.5 kJ/mol What is the overall ∆G'° for the following reaction? Phosphocreatine + ADP -> creatine + ATP

All of the following contribute to the large, negative, free-energy change upon hydrolysis of “high-energy” compounds except:

The hydrolysis of ATP has a large negative ∆G'°; nevertheless it is stable in solution due to:

Which of the following serves as the “chemical currency” of metabolism?

When a reaction proceeds with a net release of free energy, the free-energy change has a positive value and the reaction is said to be exergonic.

When, during a chemical reaction, the system changes so as to possess more free energy, the free-energy change has a positive value and the reaction is said to be exergonic.

If a reaction is exergonic converting reactants to products, then it's be endergonic converting products to reactants.

A spontaneous reactions has a large equilibrium constant.

A value of equilibrium constant equal to 4.3 x 10-2 corresponds to a non-spontaneous reaction.

The standard free energy change is often measured in kjoules or kcalories.

The conditions inside a cell or organism can be very different from these standard conditions, so ∆G values for biological reactions in vivo may vary widely from their standard free energy change (ΔG°’) values.

Changing the energy of the reactants or the products is a cellular strategy to increase to spontaneity of a reaction.

Decreasing the concentration of products ensure that a reaction is spontaneous in the forward direction.

Decreasing the concentration of reactants ensure that a reaction is spontaneous in the backwards direction.

The free-energy change depends both on the nature and the initial concentration of reactants and products.

The free energy changes of reactions that have a common intermediate can be multiplied to provide the total free energy change.

The positive value of ΔG°' predicts that, in any conditions, the reaction will tend not to proceed spontaneously in the direction written.

The energy of ATP is

The hydrolysis of ATP

ATP can be stored for long time and then used but the cell to provide chemical energy

ATP contains

Hydrolysis of the alpha phosphate group release the largest amount of energy

The synthesis of ATP from ADP and Pi is an endergonic reaction.

The free energy necessary for the synthesis of ATP is provided when carbon containing molecules undergo exergonic reactions such as oxidation reactions.

The hydrolysis of one mole GTP provides 30 kJ in standard conditions.

Pyrophosphate contains

The products of hydrolysis of ATP are more unstable that ATP

The repulsion between the four negative charges of the phosphate groups is greater in the reactants of the hydrolysis reaction of ATP.

The orthophosphate ion is stabilized by resonance.

The transfer of a phosphoryl group to a compound puts free energy into that compound, making it more stable.

Phosphorylation usually occurs when the phosphorous of the phosphoryl group reacts with an electrophile, such a the oxygen of an hydroxyl group of an alcohol.

Phosphorylation reactions are catalyzed by kinases.

Magnesium is a coenzyme.

The binding of magnesium to ATP makes the hydrolysis reaction more exergonic.

Inorganic polyphosphate is store in the cytosol.

ATP has the highest phosphoryl-transfer potential among phosphoryl containing molecules.

The formation of ATP (or GTP) by the direct transfer of a phosphoryl group to ADP (or GDP) is called substrate level phosphatase.

A phosphorylated compound is considered a high energy compound.

The breakdown of a “super-high-energy compound”, can release the energy necessary for the synthesis of ATP from ADP and Pi.

In the cell, ATP carries 4 positive charges.