DG1:The F₁F - ATP synthase is a molecular machine that converts the proton motiveforce into enzymatic activity.a. Discuss the assembly of the F, subunit and describe the role each componentplays in the function of the ATP synthase complex.b. Describe the proton path that results in rotation within the F₁F-ATP synthase.c. Explain how the F subunit contributes to the binding change mechanism.

The molecular device known as F1F0-ATP synthase transforms the proton motive force into enzymatic…

Answered: The F₁F. - ATP synthase is a molecular…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter26: Synthesis And Degradation Of Nucleotides

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Problem 21P

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A.What is the Result of the sodium potassium ATPase activity in the cell? B.What mechanism does the sodium potassium ATPase use to achieve this result? C. Why is the above-mentioned change in affinity critical for the sodium potassium ATPase to perform its function?
.Intramitochondrial ATP concentrations are about 5 mM, and phosphate con- centration 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 concentration of ATP plus half the concentration of ADP divided by the total adenine nucleotide concentration: [ATP] + 1/2[ADP] [ATP] + [ADP] + [AMP]
A4. what conformational state is stabilized by y in atp synthase? why might achieving this state require energy input from the pmf?
Explain the role and functioning of chaperone proteins. Explain, why several chaperones (chaperonins) possess an ATPase activity?
a. Use the values in Problem 23.31 to calculate the energy change in the following reaction. fructose 1,6-bisphosphate + ADP--------> fructose 6-phosphate + ATP b. Is this reaction energetically favorable or unfavorable? c. Write this reaction using curved arrow symbolism. d. Can this reaction be used to synthesize ATP from ADP? Explain.
A. Explain why it is important that an energy producing pathway contains at least one regulatory enzyme, you can use either glycolysis or TCA enzymes to discuss this answer B. The first step in glycolysis involves the conversion of glucose to glucose-6- phosphate. Briefly explain how this reaction occurs as it is an endergonic reaction. C. Why is it important that the cell has a number of different high-energy biomolecules?
a. b. C. Sphingosine-1-phosphate (SPP) has recently been discovered to be important for cell survival. The synthesis of SPP form sphingosine and ATP is catalyzed by the enzyme sphingosine kinase. An understanding of the kinetics of the sphingosine kinase reaction may be important in the development of drugs to treat cancer. The velocity of the sphingosine kinase reaction was measured in the presence (5 µM) and absence of threo-sphingosine, a stereoisomer of sphingosine. The results are shown below. The sphingosine kinase used in all the reactions was 10 mg. Sphingosine (uM) 2.5 3.5 5 10 20 50 vo (mg. min-¹) (no inhibitor) 32.3 40 50.8 72 87.7 115.4 What are the KM and V MAX in the presence and absence of the inhibitor? What kind of an inhibitor is threo-sphingosine? What is the K₁ value? What is the Keat (turn over number)? vo (mg. min-¹) (with threo-sphingosine) 7.6 10.5 14.6 25.4 43.9 70.8
5. You discover a new cysteine protease similar to papain. Cysteine proteases are proteolytic enzymes that utilize a cysteine residue in the active site for the nucleophilic attack of a peptide bond, while a second residue acts as a base for proton abstraction in the reaction (acid base catalysis). In this novel enzyme the pKa of the cysteine residue is significantly lowered by the active site environment to pKa=4. a. Knowing that the protease shows highest activity between pH 4-6, what could be the identity of the base residue acting as a in the reaction? Explain and write the expected mechanism for the reaction. SH он
Saccharides: Using the following substrates, estimate the net ATP yield after glycolytic pathway, Kreb’s cycle and electron transport chain. Assume that the estimate for ATP yield per mole of NADH is 3 moles of ATP, while 1 mole of FADH2 is equivalent to 2 moles of ATP, and one mole of GTP is equivalent to one mole of ATP. Show all pertinent solutions and determine: a) ATP used, b) ATP produced, and c) Net ATP. Based on your solutions, rank the substrates based on increasing yield of ATP Two moles of fructose-1,6-biphosphate
Saccharides: Using the following substrates, estimate the net ATP yield after glycolytic pathway, Kreb’s cycle and electron transport chain. Assume that the estimate for ATP yield per mole of NADH is 3 moles of ATP, while 1 mole of FADH2 is equivalent to 2 moles of ATP, and one mole of GTP is equivalent to one mole of ATP. Show all pertinent solutions and determine: a) ATP used, b) ATP produced, and c) Net ATP. Based on your solutions, rank the substrates based on increasing yield of ATP 1. Three moles of glucose-6-phosphate 2. Four moles of pyruvic acid
Saccharides: Using the following substrates, estimate the net ATP yield after glycolytic pathway, Kreb’s cycle and electron transport chain. Assume that the estimate for ATP yield per mole of NADH is 3 moles of ATP, while 1 mole of FADH2 is equivalent to 2 moles of ATP, and one mole of GTP is equivalent to one mole of ATP. Show all pertinent solutions and determine: a) ATP used, b) ATP produced, and c) Net ATP. Based on your solutions, rank the substrates based on increasing yield of ATP 1. Three moles of glucose-6-phosphate
Saccharides: Using the following substrates, estimate the net ATP yield after glycolytic pathway, Kreb’s cycle and electron transport chain. Assume that the estimate for ATP yield per mole of NADH is 3 moles of ATP, while 1 mole of FADH2 is equivalent to 2 moles of ATP, and one mole of GTP is equivalent to one mole of ATP. Show all pertinent solutions and determine: a) ATP used, b) ATP produced, and c) Net ATP. Based on your solutions, rank the substrates based on increasing yield of ATP Five moles of Acetyl coenzyme A

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