V-class proton pumps run backward relative to the F-class ATP synthase. Consider the cartoon, which shows the conformations of the beta-subunits andATPIADP + Pj of the F-class synthase. Which of the following associations between the conformation of the beta subunit and ATP/ADP + P¡ is correct for V-Binding Change MechanismloosebindingADP+PATPATPclass pumps?C repeatADP+ P,ADPАТРtightbindingАТР+PоpenАТРO The open conformation releases ATP.Hydrolysis of ATP to ADP + P¡ drives the change from tight to loose.O Binding of ADP + P¡ drives change from open to loose.Hydrolysis of ATP to ADP + Pj drives the change from open to loose.

There are three classes of ATPases pumps based on the difference in structure and the type of ion…

Answered: V-class proton pumps run backward…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter20: Electron Transport And Oxidative Phosphorylation

Section: Chapter Questions

Problem 19P

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Figure 27.3 illustrates the response of R (ATP-regenerating) and U (ATP-utilizing) enzymes to energy charge. a. Would hexokinase be an R enzyme or a U enzyme? Would glutamine: PRPP amidotransferase, the second enzyme in purine biosynthesis, be an R enzyme or a U enzyme? b. If energy charge = 0.5: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low? c. If energy charge = 0.95: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low?
How many protons are required to synthesize one ATP by F1F0-ATPase containing (a) 10 or (b) 15 c subunits?
ATP Synthase contains with in it one of the most conserved residues in a protein we know. Asp 61. This is the amino acid that carries the proton. a. Why would this residue be so highly conserved? What would happen if a mutation occurred that would change Asp to Ala? b. At the end of one spin of ATP synthase when the proton is in a position to leave to the intermembrane space the Asp comes into close contact with another very highly conserved residue Arg 210. Explain how this Arg residue could help the proton attached to Asp to leave. Hint think pKa Answer both parts with good explanation
An arginine residue (Arg 210) in the a subunit of the E. coli ATP synthase is near the aspartate residue (Asp 61) in the matrix-side proton channel. How might Arg 210 assist proton flow?
Intramitochondrial ATP concentrations are about 5 mM, and phosphate 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 ∆G 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.
Some enzymes can catalyze a reaction involving NADH but cannot catalyze a reaction that uses NADPH. Why may this be? When the substrate concentration is below the Km for an enzyme, what “order” will best explain thereaction? Explain.The cells that line the intestine have a transporter called GLUT5. While it can transport both fructose and glucose but has a much lower Km for fructose. Describe a physiological situation where the GLUT5 transporter is transporting fructose and glucose at the same rate. [consider using a graph to support your answer]
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Calculate the amount of ATP that be needed to be converted to ASP to pump 1mol of protons across a membrane from a solution of pH8 to pH6. (pH values are unchanged during the process). Where T=298K
Describe the conformational changes (including substrates that bind to the different conformations) that occur in the F1 domain of ATP Synthase that result from protons flowing through the Fo domain down their concentration gradient:
Explain why the coupled reaction ATP → ADP + Pi in the P-class ion pump mechanism does not involve direct hydrolysis of the phosphoanhydride bond.
Intramitochondrial ATP concentrations are about 5 mM, and phosphate concentration is about 10 mM. Consider that ADP is five times more abundant than AMP. a. Calculate the molar concentrations of ADP and AMP at an energy charge of 0.85. b. Calculate ∆G' for ATP hydrolysis under these conditions (∆G0' for ATP hydrolysis is -32.2 kJ/mol) The energy charge is defined as ( [ATP] + 1/2 [ADP] ) / ( [ATP] + [ADP] + [AMP] )
If a small amount of ATP labeled with radioactive phosphorus in the terminal position, [γ-32P]ATP, is added to a yeast extract, about half of the 32P activity is found in Pi within a few minutes, but the concentration of ATP remains unchanged. Explain. If the same experiment is carried out using ATP labeled with 32P in the central position, [β-32P]ATP, the 32P does not appear inPi within such a short time. Why?

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