Choose any/all that apply to the proton-motive force and ATP synthesis.The active pumping of protons through ATP synthase against their concentration gradientprovides the energy needed for ATP synthesis.Rotation of the y subunit creates conformational changes in the active sites of ATP synthasethat drive the release of ATP from the enzyme.Each 3 subunit of ATP synthase has a distinct amino acid sequence that accounts for thethree different active sites present in the enzyme.The ATP molecules produced from the pair of electrons provided by NADH have greaterpotential energy than the ATP molecules produced from the pair of electrons provided byFADH₂.Inhibition of either ATP synthase or ATP translocase will stop flux through the electron-transport chain.

The active pumping of protons through ATP synthase against their concentration gradient provides the…

Answered: Choose any/all that apply to the…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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OOC H H fumarase Fumarate S-malate What class of enzyme most likely catalyzes the reaction shown in the figure? choose the one best answer) Oxidoreductase COO H₂O HR IIII... Hs OOC OH COO IIIH
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Each of the molecules below can be used a a source of energy to make ATP. For each of the following, indicate HOW MANY ATP could be made from one molecule of the following. For each, explain your logic (show your work). Acetyl-CoA: Pyruvate: FADH2: Glucose-6 phosphate: Phosphoenolpyruvate: NADH: GTP:
The induced-fit theory aims to explain how the interactions between an enzyme and a sub- strate facilitate the catalysis of chemical reactions. Which of the following properties of enzyme-substrate interaction best explains enzymatic catalysis according to the induced-fit model? A B с D Environmental conditions can alter the affinity between a substrate and an enzyme by changing the conformation of the enzyme. Conformation changes in both the enzyme and the substrate due to their chemical in- teractions lower the activation energy of the catalyzed reactions. The interactions between an enzyme and a substrate depend on both structural and chemical compatibility and are therefore highly specific. Enzymes remain chemically unaltered between cycles of enzymatic catalysis while sub- strates are transformed into products.
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V-class proton pumps run backward relative to the F-class ATP synthase. Consider the cartoon, which shows the conformations of the beta-subunits and ATPIADP + 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 Mechanism loose binding ADP+P ATP ATP class pumps? C repeat ADP + P, ADP АТР tight binding АТР +P оpen АТР O 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.
i submitted this 3 times in bartleby and everyone gave differnt answers please answer correctly
The highest energy point of the serine protease reaction is the formation of the tetrahedral oxyanion intermediate on the original carbonyl carbon of the scissile peptide bond. True or False? DIPF is an irreversible inhibitor of serine proteases. True or False? The acyl-enzyme intermediate is the transition state of the reaction. True or False? Serine proteases are classified as isomerases. True or False?
Which of the following conditions will produce active glycogen phosphorylase? AMP АТР Phosphorylation of Serine 14 Glucose Glucose-6-Phosphate Phosphorylation of Serine 14 and AMP Phosphorylation of Serine 14 and ATP
Many enzyme mechanisms involve transferring protons. Sidechains of an enzyme can act as catalytic acids or catalytic bases in this process. The figure below shows a step in the reaction by the enzyme triose phosphate isomerase. Glu165 group. -OH Would a catalytic acid gain or lose a proton? Which sidechain in the mechanism is acting as a catalytic acid? co CH,OPO, 2- Activity remaining (%) Would a catalytic base gain or lose a proton? Which sidechain in the mechanism is acting as a catalytic base? 100 Curve I 8 Glu¹65 9 Below are two pH rate profiles showing the percent activity as a function of pH. Answer the questions below about how these curves relate to the mechanism of triose phosphate isomerase. Remember what fraction of a titratable group is unprotonated at the pka. 10 OH In this reaction a carbonyl is converted into an enol intermediate. Circle the enol 100 Activity remaining (%) H Curve 2 CIOH CIOH CH₂OPO,²- 8 9 N N 10 7 pH PH i) Which of these curves shows the pH rate…
Enzyme activity is dependent on many factors. List at least three different factors that could negatively impact enzyme activity and describe one use for each instance in the body. (IE. Oxycontin binds to enzyme active sites responsible for transferring pain signals, thus would be considered a
The F-class ATP synthase and the V-class proton pumps are similar in many ways. How are they different? their subunit composition the ion with which they interact none of the above their subcellular localization

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