Which is the correct link between conformation of the beta-subunit of the F1 component of the ATP synthase and ADP+P¡ or ATP? loose Binding Change Mechanism binding ATP ADP+P. ATP C repeat ADP + P, ATP ATP ADP +P, tight binding open ATP loose => binding ADP+Pj open => catalyzes ADP+P¡ into ATP O tight => releases ATP open => releases ADP+P¡ O O

Which is the correct link between conformation of the beta-subunit of the F1 component of the ATP synthase and ADP+P¡ or ATP? loose Binding Change Mechanism binding ATP ADP+P. ATP C repeat ADP + P, ATP ATP ADP +P, tight binding open ATP loose => binding ADP+Pj open => catalyzes ADP+P¡ into ATP O tight => releases ATP open => releases ADP+P¡ O O

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter18: Glycolysis

Section: Chapter Questions

Problem 21P

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Similar questions

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:
How many protons are required to synthesize one ATP by F1F0-ATPase containing (a) 10 or (b) 15 c subunits?
Enzymes normally enhance the rates of biochemical reactions by preferentially binding and stabilizing the transition states rather than either the substrates or the products of a reaction. The F|-subunit of ATP synthase does not fit this norm so well as tight binding to ATP rather than a transition state is employed to make ATP. Explain the binding-change model of the mechanism of ATP-synthase. How and why is the proton-motive force used in the reaction cycle of ATP synthase?
If actively respiring mitochondria are exposed to an inhibitor of ATPADP translocase, the electrontransport chain ceases to operate. Why?
In performing its function does mt ATP synthase require other enzymes to be involved during its function and if so what are the enzymes?
The ∆G for the streaming of H+ down the concentration gradient that powers ATP synthase is Positive Or Negative
In the rete mirabile serving the red swimming muscles oftunas, some key enzymes of catabolism show gradients ofconcentration: They are more concentrated at the cold end of therete, and less concentrated at the warm end. These variationsparallel variations that are often seen in the thermal acclimationof poikilotherms, when enzyme concentrations rise duringacclimation to cold and fall during acclimation to heat. Whatdo you think could be some of the reasons for these spatial andtemporal variations in enzyme concentration? Why not havethe highest observed enzyme concentrations everywhere at alltimes?
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?
The Relative Efficiency of ATP Synthesis in Noncyclic versus Cyclic Photophosphorylation If noncyclic photosynthetic electron transport leads to the translocation of 7 H+/2e- and cyclic photosynthetic electron transport leads to the translocation of 2 H+/e-, what is the relative photosynthetic efficiency of ATP synthesis (expressed as the number of photons absorbed per ATP synthesized) for noncyclic versus cyclic photophosphorylation? (Assume that the CF1CF0-ATP synthase yields 3 ATP/14 H+.)
Whatis the main idea behind the conformational coupling mechanism for ATP synthase? Describe the three conformational states.
Which of the following statements is false concerning the ‘tight binding site’ of ATP Synthase within the natural environment of the mitochondria? Group of answer choices ATP is released from the tight binding site This is a binding site found within an αβ subunits of the F1 portion of ATP Synthase The tight binding forces the reaction of ADP + Pi → ATP The tight binding site has the lowest KM for ATP
x 'x Paragraph Font Activate ures of Word have been disabled because it hasn't been activated. Use the lettered items below to correctly identify the numbered items (86 to 97) in the dia- "Io aoo) an ouo sasaodsar mod proay uRS 6 NADH 2 ATP (net) 2 NADH 36 or 38 ATP 6 ATP 2 ATP 18 ATP 4 ATP 4 FADH, 4 or 6 ATP 2 FADH, # ATP ascon glycolysis 88 68 Pyruvate L6 06 acetyl CoA 91 Krebs 93 92 cycle 94 95 Total Theoretical ATP Yield%3D 96