Lecture 23 Oxidative Phosphorylation Flashcards
(37 cards)
in the ETC where are you pumping protons to?
you are pumping protons from the matrix into the intermembrane space
why are there so many folds of the intermembrane?
to maximize surface area to do the most ETC and ATP synthase as possibe
Is e- transport requires for ATP synthesis?
no, if you maintain proton gradient, then your good.
What is valinomycin?
an ionophore that can carry K+ through the membrane down its chemical gradient
what does complex 5 do? in terms of proton gradient
uses the proton gradient produced by the ETC to move proteins down its concentration gradient from the intermembrane space back into the matrix to make ATP
What is the “N” side of the membrane?
the matrix, which is the negative of the membrane
What is the “P” side of the membrane?
the intermembrane space, which is Positive (bc you pumped all those protons over there)
What is another name for atp synthase that’s not complex 5?
FoF1 ATPase
Fo (membrane soluble part) part refers to the potion of the complex that is inside of the membrane and
F1 refers to the (peripheral) part of the complex that is hanging out of the matrix side (F1 potion is dissociable and you can seperate the integral and peripheral portions)
Peripheral part of ATPase
F1
Integral part of ATPase
Fo
which part of ATPase is responsible for dragging protons across the membrane?
F0
What direction is ATP synthase rotation if its doing ATP hydrolysis?
Counter clockwise
What direction is ATP synthase rotation if its synthesizing ATP?
Clockwise
Does ATP synthase rotate differently depending on if its synthesizing of hydrolyzing ATP
yas queen I would just be doing the reverse reaction so it would just move backwards
Why and how does Fo Rotate?
because you have a continuous sexy proton gradient each H+ that moves into F0 is met with an aspartic acid that get protonated by the H+, and as more H+ come, the deprotonated aspartic acids grab the protons causing the protonated apratice acids to move out of the way and rotate counter clockwise (this is talking about if you’re doing synthesis of course) kind of like a revolving door rat race situation
Why is the F₀ portion of ATP synthase named “F₀”
named for its sensitivity to Oligomycin, an antibiotic that specifically stops ATP synthase by binding to the Fo which “puts a wrench in the revolving door” and keeps it from moving protons
how many diffrent Alpha and beta dimers are there in the F1 portion of the ATPase
3, like a 6 petal flower
Oligomycin
an antibiotic that binds to Fo part of ATPase and stops its form rotating and therefore stops it all together
how many protons are needed for each synthesis of ATP
4
does F1 act like a MM enzyme
No! bc the off rate (letting go of the fully formed ATP) is actually the rate limiting step (the slowest)
what makes the alpha and beta subunits change conformation to either favor binding, catalysis or release ATP
the rotation of the gamma, epsilon and C (F0) portion of the synthase by the introduction of protons
What is the ΔG (Gibbs free energy change) of moving a proton through ATP synthase (ATPase)
around -20 kj/mol
Does shutting off the ETC shut off ATP ase
yes
what do ETC uncouplers? examples? what characteristics do uncouplers have to have?
They uncomple the ETC and rip protons shutting off ATPase
-they can freely diffuse across membrane and carry H+ (they are a type of ionophore)
-they have to be hydrophobic
-they can be protonated