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nment Wiley PLUS uni Karp, Cell and Molecular Biology, 8e, Custom for old Domini

ID: 163043 • Letter: N

Question

nment Wiley PLUS uni Karp, Cell and Molecular Biology, 8e, Custom for old Dominion Universit Help I System Announcements Chapter 05, Testbank Question 52 The three catalytic sites of ATP synthase have different substrate binding affinities O have different product binding affinities at any one time are present in different conformations pass sequentially through their three different conformations all of these are correct Copyright o 2000-2017 by John Wiley & Sons, Inc. or related companies. All rights reserved

Explanation / Answer

Choice 5 is correct.

Reason: There are three functional subunits of the ATP synthase enzyme. These subunits reside in the core enzymatic units of the enzyme and perform the catalysis of ATP synthesis by utilizing proton-motive force across the F0-F1 complex of the complex 5 of elctron transport chain. Studies have shown that these three subunits undergo sequential conformational changes when ADP binds to them. The sequential loose and tight binding of the ADP to these catalytic subunits brings about generation of ATP by utilizing inorganic phosphates. As the catalysis proceeds, the ADP travels from one subunit to the another until it travels 360 degrees and finally ejects out of the complex. Functionally, each subunits acts as a different binding site and thus has differential affinities for their substrates.