You are isolating  mitochondria from insect cells and incubating in a test tube with 0.005 M FADH2, 0.05 M ADP and 0.05 M Pi. Assuming, these 3 can enter mitochondria at no cost,no glucose/products of glucose metabolism remain in the isolated mitochondria, and oxygen is present.  Part 1) If all expected reactions go to completion, how much ATP is expected formed?  (0 M)(0.02 M) (0.03 M) (0.05 M) (0.1 M) (0.005 M) (0.01 M) (0.015 M)  Part 2) The ratio of FADH2/FAD at completion of all expected reactions would be? (2) (>>2) (0) (1)  Part 3) After completion of all expected reactions, ratio of H ion concentration inside vs. outside the mitochondrial inner membrane should be?  (<1) (~1) (>1)(0)  Please provide brief explanation

Intramitochondrial ATP concentrations are about 5 mM, and phos- phate concentration is about 10 mM. If ADP is five times more abundant than AMP, calculate the molar concentrations of ADP and AMP at an energy charge of 0.85. Calculate AG for ATP hydrolysis at 37 °C under these conditions. The energy charge is the concentra- tion of ATP plus half the concentration of ADP divided by the total adenine nucleotide concentration: [ATP] + 1/2[ADP] [ATP] + [ADP] + [AMP]

Citrate and isocitrate are interconverted via the enzyme aconitase: The standard free energy change for this reaction is +6.7 kJ/mol. In my pet llama's mitochondria, the free energy change was measured to be +0.8 kJ/mol. (No llamas were harmed in this experiment!) a. Calculate the [isocitrate]/[citrate] ratio in these mitochondria. b. If [isocitrate] =0.03 mM, what is [citrate]?

1. a. Calculate the physiological DG of the reaction shown below at 37°C, as it occurs in the cytosol ofneurons, with phosphocreatine at 4.7 mM, creatine at 1.0 mM, ADP at 0.73 mM, and ATP at 2.6mM. The standard free energy change for the overall reaction is –12.5 kJ/mol. Phosphocreatine + ADP ® creatine + ATP b. The enzyme phosphoglucomutase catalyzes the conversion of glucose 1-phosphate to glucose6-phosphate. Calculate the standard free energy change of this reaction if incubation of 20 mMglucose 1-phosphate (no glucose-6 phosphate initially present) yields a final equilibrium mixtureof 1.0 mM glucose 1-phosphate and 19 mM glucose 6-phosphate at 25°C and pH 7.0.   c. If the rate of a nonenzymatic reaction is 1.2 x 10–2 μM s–1, what is the rate of the reaction at 37℃ inthe presence of an enzyme that reduces the activation energy by 30.5 kJ/mol?