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So, ATP-Synthase synthesis ATP through a mechanism of rotational

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File: fatpase-structure-dmz_0.png (40KB, 300x218px) Image search: [Google]
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So, ATP-Synthase synthesis ATP through a mechanism of rotational catalysis: if the gamma subunit rotates in one direction ATP and if it rotates in the other direction ATP is hydrolized. A really beautiful mechanism!

But why the hydrolysis of ATP doesn't pump protons to the other side? And what if the intermembrane space is more basic than the mitrocondrial matrix, would the synthase hydrolyse ATP using the downhill pump of protons because the gamma subunit would be turning the other way? (Of course the downhill pump of protons it's not necessary energetically to hydrolyse ATP but in mechanic ways it makes sense to me)
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>>9000200
Thank fuck I only need to understand small bits of photosynthesis. I pity the fools who have to study this in detail..
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>>9000200
Statistical mechanics here, ignorant of details of actual mechanisms.
Cranking the ATP pump with a chemical gradient doesn't mean destroying ATP must pump the gradient. Your exchanging internal energy to work twice, loosing heat in the process.
If the system was perfectly reversible you would have a perpetuum mobile of the second kind.
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>>9000200
>But why the hydrolysis of ATP doesn't pump protons to the other side?
They're statistically unlikely to due to the gradient.
>And what if the intermembrane space is more basic than the mitrocondrial matrix, would the synthase hydrolyse ATP using the downhill pump of protons because the gamma subunit would be turning the other way? (Of course the downhill pump of protons it's not necessary energetically to hydrolyse ATP but in mechanic ways it makes sense to me)
Yes actually.
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>>9000200
stop talking about "gamma subunits" when you clearly don't understand the most basic concepts of biology. What you're asking is honestly middle school level.

Shortly put,
ATP-synthase is a form of passive transport, it's a transporter that transports molecules/ions (ions in this case) without (directly) requiring ATP to function. It's able to do this as the H+ is transported along with the H+ gradiƫnt. Remember osmosis?

Ofcourse the H+ gradiƫnt has to be sustained. That's the job of the 3 membrane complexes (and 2 mobile carriers) that form the electron transport route and is also the reason why you need the initial energy that is created by your krebs cycle.
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>>9001565
Not statistically unlikely, literally impossible.

ATP-synthase is not a form of channeled transport (which you're probably confusing it with somehow)
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File: voetvoet.png (14KB, 286x84px) Image search: [Google]
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>>9001602 Really? Actually I think you misunderstood what I said. I know the Fo domain does not require ATP to function, buddy. But if the mitrochondrial matrix is in the same pH that the intermembrane space, the F1 domain may hydrolyze ATP and pump H+ outside. Voet's Biochemistry can confirm what I said. (page 858, 4th edition)
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>>9001754
This should only happen in bacteria under anaerobic conditions where the Krebs cycle isn't running. I don't understand what purpose it would serve though unless it creates a positive atp synthesis balance. Since I've never heard of it happening in animal cells it most likely isn't that energetically favorable.
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>>9001754
... the screenshot you show is an F-type ATP-ase.

The V-type ATP-ase that you see in mitochondrias could theoretically change to an F-type pump but then it'd require ATP to function which is counter productive and not possible in this situation.

If the electron transport route stops functioning due to a defect (not sure if that's even possible without the cell going in apoptosis), then the H+ gradient will cease to exist and the pH will be isotone (neutral).

There is literally no purpose in using ATP to pump H+ into the matrix of the mitochondria. It'd actually just kill the organel and it'd just waste ATP for no reason. So it will not do that as it won't get signalled to do so.
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The motor protein complex for prokaryotic flagellum uses the same pH gradient mechanism to spin so it's kind of like an atp synthase stuck in reverse.
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